data_8PXQ
# 
_entry.id   8PXQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8PXQ         pdb_00008pxq 10.2210/pdb8pxq/pdb 
WWPDB D_1292132152 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8PXQ 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              jworrall@essex.ac.uk 
_pdbx_contact_author.name_first         Jonathan 
_pdbx_contact_author.name_last          Worrall 
_pdbx_contact_author.name_mi            A.R. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1863-834X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lucic, M.'       1 ? 
'Worrall, J.A.R.' 2 ? 
'Hough, M.A.'     3 ? 
'Pfalzgraf, H.'   4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SFX ferric structure of A type dye-decolourising peroxidase DtpAa' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lucic, M.'       1 ? 
primary 'Thompson, A.'    2 ? 
primary 'Worrall, J.A.R.' 3 ? 
primary 'Hough, M.A.'     4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Deferrochelatase                  44233.418 2   1.11.1.- Y389F ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ?        ?     ? ? 
3 water       nat water                             18.015    361 ?        ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Peroxidase EfeB' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTDTDSPAPAPSPSRRSLIGWGGAGLALGAAAAAGGAVAMDRAGADADPAGADAGSAVPFHGAHQAGIATPVQDRLHFAA
FDVTTEDRAAFVALLKEWTAAARRLTAGHAVGEGAYGGLPEAPPDDTGEALGLKPSRLTLTIGFGPSLFTRFGLADLRPE
ALADLPKFPGDNLDRARSGGDLCVQACADDPQVAVHAIRNLARIGFGKVVVRWSQLGFGKTSSTTPDKQTPRNLLGFKDG
TRNIAGTEKDRLDRFVWAAEKDGTPWMTGGSYLVARRIRMHIETWDRASLQEQEDVFGRDKGEGAPVGKAKERDEPFLKA
MKPDAHVRLAHPDSNGGATLLRRGYSFTDGTDGLGRLDAGLFFLAYQRDIRTGFVPVQRNLATDALNEFIQHVGSAVFAV
PPGVRDADDWWGSTLFG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDTDSPAPAPSPSRRSLIGWGGAGLALGAAAAAGGAVAMDRAGADADPAGADAGSAVPFHGAHQAGIATPVQDRLHFAA
FDVTTEDRAAFVALLKEWTAAARRLTAGHAVGEGAYGGLPEAPPDDTGEALGLKPSRLTLTIGFGPSLFTRFGLADLRPE
ALADLPKFPGDNLDRARSGGDLCVQACADDPQVAVHAIRNLARIGFGKVVVRWSQLGFGKTSSTTPDKQTPRNLLGFKDG
TRNIAGTEKDRLDRFVWAAEKDGTPWMTGGSYLVARRIRMHIETWDRASLQEQEDVFGRDKGEGAPVGKAKERDEPFLKA
MKPDAHVRLAHPDSNGGATLLRRGYSFTDGTDGLGRLDAGLFFLAYQRDIRTGFVPVQRNLATDALNEFIQHVGSAVFAV
PPGVRDADDWWGSTLFG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ASP n 
1 4   THR n 
1 5   ASP n 
1 6   SER n 
1 7   PRO n 
1 8   ALA n 
1 9   PRO n 
1 10  ALA n 
1 11  PRO n 
1 12  SER n 
1 13  PRO n 
1 14  SER n 
1 15  ARG n 
1 16  ARG n 
1 17  SER n 
1 18  LEU n 
1 19  ILE n 
1 20  GLY n 
1 21  TRP n 
1 22  GLY n 
1 23  GLY n 
1 24  ALA n 
1 25  GLY n 
1 26  LEU n 
1 27  ALA n 
1 28  LEU n 
1 29  GLY n 
1 30  ALA n 
1 31  ALA n 
1 32  ALA n 
1 33  ALA n 
1 34  ALA n 
1 35  GLY n 
1 36  GLY n 
1 37  ALA n 
1 38  VAL n 
1 39  ALA n 
1 40  MET n 
1 41  ASP n 
1 42  ARG n 
1 43  ALA n 
1 44  GLY n 
1 45  ALA n 
1 46  ASP n 
1 47  ALA n 
1 48  ASP n 
1 49  PRO n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  ASP n 
1 54  ALA n 
1 55  GLY n 
1 56  SER n 
1 57  ALA n 
1 58  VAL n 
1 59  PRO n 
1 60  PHE n 
1 61  HIS n 
1 62  GLY n 
1 63  ALA n 
1 64  HIS n 
1 65  GLN n 
1 66  ALA n 
1 67  GLY n 
1 68  ILE n 
1 69  ALA n 
1 70  THR n 
1 71  PRO n 
1 72  VAL n 
1 73  GLN n 
1 74  ASP n 
1 75  ARG n 
1 76  LEU n 
1 77  HIS n 
1 78  PHE n 
1 79  ALA n 
1 80  ALA n 
1 81  PHE n 
1 82  ASP n 
1 83  VAL n 
1 84  THR n 
1 85  THR n 
1 86  GLU n 
1 87  ASP n 
1 88  ARG n 
1 89  ALA n 
1 90  ALA n 
1 91  PHE n 
1 92  VAL n 
1 93  ALA n 
1 94  LEU n 
1 95  LEU n 
1 96  LYS n 
1 97  GLU n 
1 98  TRP n 
1 99  THR n 
1 100 ALA n 
1 101 ALA n 
1 102 ALA n 
1 103 ARG n 
1 104 ARG n 
1 105 LEU n 
1 106 THR n 
1 107 ALA n 
1 108 GLY n 
1 109 HIS n 
1 110 ALA n 
1 111 VAL n 
1 112 GLY n 
1 113 GLU n 
1 114 GLY n 
1 115 ALA n 
1 116 TYR n 
1 117 GLY n 
1 118 GLY n 
1 119 LEU n 
1 120 PRO n 
1 121 GLU n 
1 122 ALA n 
1 123 PRO n 
1 124 PRO n 
1 125 ASP n 
1 126 ASP n 
1 127 THR n 
1 128 GLY n 
1 129 GLU n 
1 130 ALA n 
1 131 LEU n 
1 132 GLY n 
1 133 LEU n 
1 134 LYS n 
1 135 PRO n 
1 136 SER n 
1 137 ARG n 
1 138 LEU n 
1 139 THR n 
1 140 LEU n 
1 141 THR n 
1 142 ILE n 
1 143 GLY n 
1 144 PHE n 
1 145 GLY n 
1 146 PRO n 
1 147 SER n 
1 148 LEU n 
1 149 PHE n 
1 150 THR n 
1 151 ARG n 
1 152 PHE n 
1 153 GLY n 
1 154 LEU n 
1 155 ALA n 
1 156 ASP n 
1 157 LEU n 
1 158 ARG n 
1 159 PRO n 
1 160 GLU n 
1 161 ALA n 
1 162 LEU n 
1 163 ALA n 
1 164 ASP n 
1 165 LEU n 
1 166 PRO n 
1 167 LYS n 
1 168 PHE n 
1 169 PRO n 
1 170 GLY n 
1 171 ASP n 
1 172 ASN n 
1 173 LEU n 
1 174 ASP n 
1 175 ARG n 
1 176 ALA n 
1 177 ARG n 
1 178 SER n 
1 179 GLY n 
1 180 GLY n 
1 181 ASP n 
1 182 LEU n 
1 183 CYS n 
1 184 VAL n 
1 185 GLN n 
1 186 ALA n 
1 187 CYS n 
1 188 ALA n 
1 189 ASP n 
1 190 ASP n 
1 191 PRO n 
1 192 GLN n 
1 193 VAL n 
1 194 ALA n 
1 195 VAL n 
1 196 HIS n 
1 197 ALA n 
1 198 ILE n 
1 199 ARG n 
1 200 ASN n 
1 201 LEU n 
1 202 ALA n 
1 203 ARG n 
1 204 ILE n 
1 205 GLY n 
1 206 PHE n 
1 207 GLY n 
1 208 LYS n 
1 209 VAL n 
1 210 VAL n 
1 211 VAL n 
1 212 ARG n 
1 213 TRP n 
1 214 SER n 
1 215 GLN n 
1 216 LEU n 
1 217 GLY n 
1 218 PHE n 
1 219 GLY n 
1 220 LYS n 
1 221 THR n 
1 222 SER n 
1 223 SER n 
1 224 THR n 
1 225 THR n 
1 226 PRO n 
1 227 ASP n 
1 228 LYS n 
1 229 GLN n 
1 230 THR n 
1 231 PRO n 
1 232 ARG n 
1 233 ASN n 
1 234 LEU n 
1 235 LEU n 
1 236 GLY n 
1 237 PHE n 
1 238 LYS n 
1 239 ASP n 
1 240 GLY n 
1 241 THR n 
1 242 ARG n 
1 243 ASN n 
1 244 ILE n 
1 245 ALA n 
1 246 GLY n 
1 247 THR n 
1 248 GLU n 
1 249 LYS n 
1 250 ASP n 
1 251 ARG n 
1 252 LEU n 
1 253 ASP n 
1 254 ARG n 
1 255 PHE n 
1 256 VAL n 
1 257 TRP n 
1 258 ALA n 
1 259 ALA n 
1 260 GLU n 
1 261 LYS n 
1 262 ASP n 
1 263 GLY n 
1 264 THR n 
1 265 PRO n 
1 266 TRP n 
1 267 MET n 
1 268 THR n 
1 269 GLY n 
1 270 GLY n 
1 271 SER n 
1 272 TYR n 
1 273 LEU n 
1 274 VAL n 
1 275 ALA n 
1 276 ARG n 
1 277 ARG n 
1 278 ILE n 
1 279 ARG n 
1 280 MET n 
1 281 HIS n 
1 282 ILE n 
1 283 GLU n 
1 284 THR n 
1 285 TRP n 
1 286 ASP n 
1 287 ARG n 
1 288 ALA n 
1 289 SER n 
1 290 LEU n 
1 291 GLN n 
1 292 GLU n 
1 293 GLN n 
1 294 GLU n 
1 295 ASP n 
1 296 VAL n 
1 297 PHE n 
1 298 GLY n 
1 299 ARG n 
1 300 ASP n 
1 301 LYS n 
1 302 GLY n 
1 303 GLU n 
1 304 GLY n 
1 305 ALA n 
1 306 PRO n 
1 307 VAL n 
1 308 GLY n 
1 309 LYS n 
1 310 ALA n 
1 311 LYS n 
1 312 GLU n 
1 313 ARG n 
1 314 ASP n 
1 315 GLU n 
1 316 PRO n 
1 317 PHE n 
1 318 LEU n 
1 319 LYS n 
1 320 ALA n 
1 321 MET n 
1 322 LYS n 
1 323 PRO n 
1 324 ASP n 
1 325 ALA n 
1 326 HIS n 
1 327 VAL n 
1 328 ARG n 
1 329 LEU n 
1 330 ALA n 
1 331 HIS n 
1 332 PRO n 
1 333 ASP n 
1 334 SER n 
1 335 ASN n 
1 336 GLY n 
1 337 GLY n 
1 338 ALA n 
1 339 THR n 
1 340 LEU n 
1 341 LEU n 
1 342 ARG n 
1 343 ARG n 
1 344 GLY n 
1 345 TYR n 
1 346 SER n 
1 347 PHE n 
1 348 THR n 
1 349 ASP n 
1 350 GLY n 
1 351 THR n 
1 352 ASP n 
1 353 GLY n 
1 354 LEU n 
1 355 GLY n 
1 356 ARG n 
1 357 LEU n 
1 358 ASP n 
1 359 ALA n 
1 360 GLY n 
1 361 LEU n 
1 362 PHE n 
1 363 PHE n 
1 364 LEU n 
1 365 ALA n 
1 366 TYR n 
1 367 GLN n 
1 368 ARG n 
1 369 ASP n 
1 370 ILE n 
1 371 ARG n 
1 372 THR n 
1 373 GLY n 
1 374 PHE n 
1 375 VAL n 
1 376 PRO n 
1 377 VAL n 
1 378 GLN n 
1 379 ARG n 
1 380 ASN n 
1 381 LEU n 
1 382 ALA n 
1 383 THR n 
1 384 ASP n 
1 385 ALA n 
1 386 LEU n 
1 387 ASN n 
1 388 GLU n 
1 389 PHE n 
1 390 ILE n 
1 391 GLN n 
1 392 HIS n 
1 393 VAL n 
1 394 GLY n 
1 395 SER n 
1 396 ALA n 
1 397 VAL n 
1 398 PHE n 
1 399 ALA n 
1 400 VAL n 
1 401 PRO n 
1 402 PRO n 
1 403 GLY n 
1 404 VAL n 
1 405 ARG n 
1 406 ASP n 
1 407 ALA n 
1 408 ASP n 
1 409 ASP n 
1 410 TRP n 
1 411 TRP n 
1 412 GLY n 
1 413 SER n 
1 414 THR n 
1 415 LEU n 
1 416 PHE n 
1 417 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   417 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SLI_2602 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces lividans 1326' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1200984 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?    'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                         ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?    'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                         ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ?    'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ?    'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                           ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                            ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   ASP 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   ?   ?   ?   A . n 
A 1 7   PRO 7   7   ?   ?   ?   A . n 
A 1 8   ALA 8   8   ?   ?   ?   A . n 
A 1 9   PRO 9   9   ?   ?   ?   A . n 
A 1 10  ALA 10  10  ?   ?   ?   A . n 
A 1 11  PRO 11  11  ?   ?   ?   A . n 
A 1 12  SER 12  12  ?   ?   ?   A . n 
A 1 13  PRO 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  ?   ?   ?   A . n 
A 1 15  ARG 15  15  ?   ?   ?   A . n 
A 1 16  ARG 16  16  ?   ?   ?   A . n 
A 1 17  SER 17  17  ?   ?   ?   A . n 
A 1 18  LEU 18  18  ?   ?   ?   A . n 
A 1 19  ILE 19  19  ?   ?   ?   A . n 
A 1 20  GLY 20  20  ?   ?   ?   A . n 
A 1 21  TRP 21  21  ?   ?   ?   A . n 
A 1 22  GLY 22  22  ?   ?   ?   A . n 
A 1 23  GLY 23  23  ?   ?   ?   A . n 
A 1 24  ALA 24  24  ?   ?   ?   A . n 
A 1 25  GLY 25  25  ?   ?   ?   A . n 
A 1 26  LEU 26  26  ?   ?   ?   A . n 
A 1 27  ALA 27  27  ?   ?   ?   A . n 
A 1 28  LEU 28  28  ?   ?   ?   A . n 
A 1 29  GLY 29  29  ?   ?   ?   A . n 
A 1 30  ALA 30  30  ?   ?   ?   A . n 
A 1 31  ALA 31  31  ?   ?   ?   A . n 
A 1 32  ALA 32  32  ?   ?   ?   A . n 
A 1 33  ALA 33  33  ?   ?   ?   A . n 
A 1 34  ALA 34  34  ?   ?   ?   A . n 
A 1 35  GLY 35  35  ?   ?   ?   A . n 
A 1 36  GLY 36  36  ?   ?   ?   A . n 
A 1 37  ALA 37  37  ?   ?   ?   A . n 
A 1 38  VAL 38  38  ?   ?   ?   A . n 
A 1 39  ALA 39  39  ?   ?   ?   A . n 
A 1 40  MET 40  40  ?   ?   ?   A . n 
A 1 41  ASP 41  41  ?   ?   ?   A . n 
A 1 42  ARG 42  42  ?   ?   ?   A . n 
A 1 43  ALA 43  43  ?   ?   ?   A . n 
A 1 44  GLY 44  44  ?   ?   ?   A . n 
A 1 45  ALA 45  45  ?   ?   ?   A . n 
A 1 46  ASP 46  46  ?   ?   ?   A . n 
A 1 47  ALA 47  47  ?   ?   ?   A . n 
A 1 48  ASP 48  48  ?   ?   ?   A . n 
A 1 49  PRO 49  49  ?   ?   ?   A . n 
A 1 50  ALA 50  50  ?   ?   ?   A . n 
A 1 51  GLY 51  51  ?   ?   ?   A . n 
A 1 52  ALA 52  52  ?   ?   ?   A . n 
A 1 53  ASP 53  53  ?   ?   ?   A . n 
A 1 54  ALA 54  54  ?   ?   ?   A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  HIS 61  61  61  HIS HIS A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 PRO 146 146 146 PRO PRO A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 CYS 183 183 183 CYS CYS A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 CYS 187 187 187 CYS CYS A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 TRP 213 213 213 TRP TRP A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 GLN 215 215 215 GLN GLN A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 PRO 226 226 226 PRO PRO A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 ARG 232 232 232 ARG ARG A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 PHE 237 237 237 PHE PHE A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 ARG 251 251 251 ARG ARG A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 PHE 255 255 255 PHE PHE A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 ASP 262 262 262 ASP ASP A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 PRO 265 265 265 PRO PRO A . n 
A 1 266 TRP 266 266 266 TRP TRP A . n 
A 1 267 MET 267 267 267 MET MET A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 TYR 272 272 272 TYR TYR A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 MET 280 280 280 MET MET A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 THR 284 284 284 THR THR A . n 
A 1 285 TRP 285 285 285 TRP TRP A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 GLN 293 293 293 GLN GLN A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 ARG 299 299 299 ARG ARG A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 VAL 307 307 307 VAL VAL A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 ARG 313 313 313 ARG ARG A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 PRO 316 316 316 PRO PRO A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 MET 321 321 321 MET MET A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 PRO 323 323 323 PRO PRO A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 HIS 326 326 326 HIS HIS A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 ASP 333 333 333 ASP ASP A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 ASN 335 335 335 ASN ASN A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 ARG 342 342 342 ARG ARG A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 PHE 362 362 362 PHE PHE A . n 
A 1 363 PHE 363 363 363 PHE PHE A . n 
A 1 364 LEU 364 364 364 LEU LEU A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 TYR 366 366 366 TYR TYR A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ILE 370 370 370 ILE ILE A . n 
A 1 371 ARG 371 371 371 ARG ARG A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 PHE 374 374 374 PHE PHE A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 VAL 377 377 377 VAL VAL A . n 
A 1 378 GLN 378 378 378 GLN GLN A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 ASP 384 384 384 ASP ASP A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 ASN 387 387 387 ASN ASN A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 PHE 389 389 389 PHE PHE A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 GLN 391 391 391 GLN GLN A . n 
A 1 392 HIS 392 392 392 HIS HIS A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 VAL 397 397 397 VAL VAL A . n 
A 1 398 PHE 398 398 398 PHE PHE A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 PRO 401 401 401 PRO PRO A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 GLY 403 403 403 GLY GLY A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 ASP 406 406 406 ASP ASP A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 ASP 408 408 408 ASP ASP A . n 
A 1 409 ASP 409 409 409 ASP ASP A . n 
A 1 410 TRP 410 410 410 TRP TRP A . n 
A 1 411 TRP 411 411 411 TRP TRP A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 THR 414 414 414 THR THR A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 PHE 416 416 416 PHE PHE A . n 
A 1 417 GLY 417 417 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   ASP 3   3   ?   ?   ?   B . n 
B 1 4   THR 4   4   ?   ?   ?   B . n 
B 1 5   ASP 5   5   ?   ?   ?   B . n 
B 1 6   SER 6   6   ?   ?   ?   B . n 
B 1 7   PRO 7   7   ?   ?   ?   B . n 
B 1 8   ALA 8   8   ?   ?   ?   B . n 
B 1 9   PRO 9   9   ?   ?   ?   B . n 
B 1 10  ALA 10  10  ?   ?   ?   B . n 
B 1 11  PRO 11  11  ?   ?   ?   B . n 
B 1 12  SER 12  12  ?   ?   ?   B . n 
B 1 13  PRO 13  13  ?   ?   ?   B . n 
B 1 14  SER 14  14  ?   ?   ?   B . n 
B 1 15  ARG 15  15  ?   ?   ?   B . n 
B 1 16  ARG 16  16  ?   ?   ?   B . n 
B 1 17  SER 17  17  ?   ?   ?   B . n 
B 1 18  LEU 18  18  ?   ?   ?   B . n 
B 1 19  ILE 19  19  ?   ?   ?   B . n 
B 1 20  GLY 20  20  ?   ?   ?   B . n 
B 1 21  TRP 21  21  ?   ?   ?   B . n 
B 1 22  GLY 22  22  ?   ?   ?   B . n 
B 1 23  GLY 23  23  ?   ?   ?   B . n 
B 1 24  ALA 24  24  ?   ?   ?   B . n 
B 1 25  GLY 25  25  ?   ?   ?   B . n 
B 1 26  LEU 26  26  ?   ?   ?   B . n 
B 1 27  ALA 27  27  ?   ?   ?   B . n 
B 1 28  LEU 28  28  ?   ?   ?   B . n 
B 1 29  GLY 29  29  ?   ?   ?   B . n 
B 1 30  ALA 30  30  ?   ?   ?   B . n 
B 1 31  ALA 31  31  ?   ?   ?   B . n 
B 1 32  ALA 32  32  ?   ?   ?   B . n 
B 1 33  ALA 33  33  ?   ?   ?   B . n 
B 1 34  ALA 34  34  ?   ?   ?   B . n 
B 1 35  GLY 35  35  ?   ?   ?   B . n 
B 1 36  GLY 36  36  ?   ?   ?   B . n 
B 1 37  ALA 37  37  ?   ?   ?   B . n 
B 1 38  VAL 38  38  ?   ?   ?   B . n 
B 1 39  ALA 39  39  ?   ?   ?   B . n 
B 1 40  MET 40  40  ?   ?   ?   B . n 
B 1 41  ASP 41  41  ?   ?   ?   B . n 
B 1 42  ARG 42  42  ?   ?   ?   B . n 
B 1 43  ALA 43  43  ?   ?   ?   B . n 
B 1 44  GLY 44  44  ?   ?   ?   B . n 
B 1 45  ALA 45  45  ?   ?   ?   B . n 
B 1 46  ASP 46  46  ?   ?   ?   B . n 
B 1 47  ALA 47  47  ?   ?   ?   B . n 
B 1 48  ASP 48  48  ?   ?   ?   B . n 
B 1 49  PRO 49  49  ?   ?   ?   B . n 
B 1 50  ALA 50  50  ?   ?   ?   B . n 
B 1 51  GLY 51  51  ?   ?   ?   B . n 
B 1 52  ALA 52  52  ?   ?   ?   B . n 
B 1 53  ASP 53  53  ?   ?   ?   B . n 
B 1 54  ALA 54  54  ?   ?   ?   B . n 
B 1 55  GLY 55  55  ?   ?   ?   B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  PRO 59  59  59  PRO PRO B . n 
B 1 60  PHE 60  60  60  PHE PHE B . n 
B 1 61  HIS 61  61  61  HIS HIS B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  PRO 71  71  71  PRO PRO B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  ARG 75  75  75  ARG ARG B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  PHE 78  78  78  PHE PHE B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  TRP 98  98  98  TRP TRP B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 ALA 100 100 100 ALA ALA B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 HIS 109 109 109 HIS HIS B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 GLU 113 113 113 GLU GLU B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 GLY 117 117 117 GLY GLY B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 PRO 120 120 120 PRO PRO B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 PRO 123 123 123 PRO PRO B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 ASP 126 126 126 ASP ASP B . n 
B 1 127 THR 127 127 127 THR THR B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 LYS 134 134 134 LYS LYS B . n 
B 1 135 PRO 135 135 135 PRO PRO B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 ARG 137 137 137 ARG ARG B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 THR 139 139 139 THR THR B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 PRO 146 146 146 PRO PRO B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 PHE 149 149 149 PHE PHE B . n 
B 1 150 THR 150 150 150 THR THR B . n 
B 1 151 ARG 151 151 151 ARG ARG B . n 
B 1 152 PHE 152 152 152 PHE PHE B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 LEU 154 154 154 LEU LEU B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ARG 158 158 158 ARG ARG B . n 
B 1 159 PRO 159 159 159 PRO PRO B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 PRO 166 166 166 PRO PRO B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ASN 172 172 172 ASN ASN B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 ASP 174 174 174 ASP ASP B . n 
B 1 175 ARG 175 175 175 ARG ARG B . n 
B 1 176 ALA 176 176 176 ALA ALA B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 CYS 183 183 183 CYS CYS B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 CYS 187 187 187 CYS CYS B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 PRO 191 191 191 PRO PRO B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 ARG 199 199 199 ARG ARG B . n 
B 1 200 ASN 200 200 200 ASN ASN B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 ALA 202 202 202 ALA ALA B . n 
B 1 203 ARG 203 203 203 ARG ARG B . n 
B 1 204 ILE 204 204 204 ILE ILE B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 PHE 206 206 206 PHE PHE B . n 
B 1 207 GLY 207 207 207 GLY GLY B . n 
B 1 208 LYS 208 208 208 LYS LYS B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 TRP 213 213 213 TRP TRP B . n 
B 1 214 SER 214 214 214 SER SER B . n 
B 1 215 GLN 215 215 215 GLN GLN B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 PHE 218 218 218 PHE PHE B . n 
B 1 219 GLY 219 219 219 GLY GLY B . n 
B 1 220 LYS 220 220 220 LYS LYS B . n 
B 1 221 THR 221 221 221 THR THR B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 PRO 226 226 226 PRO PRO B . n 
B 1 227 ASP 227 227 227 ASP ASP B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 THR 230 230 230 THR THR B . n 
B 1 231 PRO 231 231 231 PRO PRO B . n 
B 1 232 ARG 232 232 232 ARG ARG B . n 
B 1 233 ASN 233 233 233 ASN ASN B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 LEU 235 235 235 LEU LEU B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 PHE 237 237 237 PHE PHE B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 THR 241 241 241 THR THR B . n 
B 1 242 ARG 242 242 242 ARG ARG B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 ASP 250 250 250 ASP ASP B . n 
B 1 251 ARG 251 251 251 ARG ARG B . n 
B 1 252 LEU 252 252 252 LEU LEU B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 ARG 254 254 254 ARG ARG B . n 
B 1 255 PHE 255 255 255 PHE PHE B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 TRP 257 257 257 TRP TRP B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 GLU 260 260 260 GLU GLU B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 ASP 262 262 262 ASP ASP B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 PRO 265 265 265 PRO PRO B . n 
B 1 266 TRP 266 266 266 TRP TRP B . n 
B 1 267 MET 267 267 267 MET MET B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 GLY 269 269 269 GLY GLY B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 TYR 272 272 272 TYR TYR B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 VAL 274 274 274 VAL VAL B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 ARG 276 276 276 ARG ARG B . n 
B 1 277 ARG 277 277 277 ARG ARG B . n 
B 1 278 ILE 278 278 278 ILE ILE B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 MET 280 280 280 MET MET B . n 
B 1 281 HIS 281 281 281 HIS HIS B . n 
B 1 282 ILE 282 282 282 ILE ILE B . n 
B 1 283 GLU 283 283 283 GLU GLU B . n 
B 1 284 THR 284 284 284 THR THR B . n 
B 1 285 TRP 285 285 285 TRP TRP B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 ARG 287 287 287 ARG ARG B . n 
B 1 288 ALA 288 288 288 ALA ALA B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 GLN 291 291 291 GLN GLN B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 GLN 293 293 293 GLN GLN B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 GLY 298 298 298 GLY GLY B . n 
B 1 299 ARG 299 299 299 ARG ARG B . n 
B 1 300 ASP 300 300 300 ASP ASP B . n 
B 1 301 LYS 301 301 301 LYS LYS B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 GLU 303 303 303 GLU GLU B . n 
B 1 304 GLY 304 304 304 GLY GLY B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 PRO 306 306 306 PRO PRO B . n 
B 1 307 VAL 307 307 307 VAL VAL B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 ALA 310 310 310 ALA ALA B . n 
B 1 311 LYS 311 311 311 LYS LYS B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 ARG 313 313 313 ARG ARG B . n 
B 1 314 ASP 314 314 314 ASP ASP B . n 
B 1 315 GLU 315 315 315 GLU GLU B . n 
B 1 316 PRO 316 316 316 PRO PRO B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 LYS 319 319 319 LYS LYS B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 MET 321 321 321 MET MET B . n 
B 1 322 LYS 322 322 322 LYS LYS B . n 
B 1 323 PRO 323 323 323 PRO PRO B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 ALA 325 325 325 ALA ALA B . n 
B 1 326 HIS 326 326 326 HIS HIS B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ARG 328 328 328 ARG ARG B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 HIS 331 331 331 HIS HIS B . n 
B 1 332 PRO 332 332 332 PRO PRO B . n 
B 1 333 ASP 333 333 333 ASP ASP B . n 
B 1 334 SER 334 334 334 SER SER B . n 
B 1 335 ASN 335 335 335 ASN ASN B . n 
B 1 336 GLY 336 336 336 GLY GLY B . n 
B 1 337 GLY 337 337 337 GLY GLY B . n 
B 1 338 ALA 338 338 338 ALA ALA B . n 
B 1 339 THR 339 339 339 THR THR B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 ARG 342 342 342 ARG ARG B . n 
B 1 343 ARG 343 343 343 ARG ARG B . n 
B 1 344 GLY 344 344 344 GLY GLY B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 SER 346 346 346 SER SER B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 THR 348 348 348 THR THR B . n 
B 1 349 ASP 349 349 349 ASP ASP B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 LEU 354 354 354 LEU LEU B . n 
B 1 355 GLY 355 355 355 GLY GLY B . n 
B 1 356 ARG 356 356 356 ARG ARG B . n 
B 1 357 LEU 357 357 357 LEU LEU B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 ALA 359 359 359 ALA ALA B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 PHE 362 362 362 PHE PHE B . n 
B 1 363 PHE 363 363 363 PHE PHE B . n 
B 1 364 LEU 364 364 364 LEU LEU B . n 
B 1 365 ALA 365 365 365 ALA ALA B . n 
B 1 366 TYR 366 366 366 TYR TYR B . n 
B 1 367 GLN 367 367 367 GLN GLN B . n 
B 1 368 ARG 368 368 368 ARG ARG B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 ILE 370 370 370 ILE ILE B . n 
B 1 371 ARG 371 371 371 ARG ARG B . n 
B 1 372 THR 372 372 372 THR THR B . n 
B 1 373 GLY 373 373 373 GLY GLY B . n 
B 1 374 PHE 374 374 374 PHE PHE B . n 
B 1 375 VAL 375 375 375 VAL VAL B . n 
B 1 376 PRO 376 376 376 PRO PRO B . n 
B 1 377 VAL 377 377 377 VAL VAL B . n 
B 1 378 GLN 378 378 378 GLN GLN B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 ALA 382 382 382 ALA ALA B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 ASP 384 384 384 ASP ASP B . n 
B 1 385 ALA 385 385 385 ALA ALA B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 ASN 387 387 387 ASN ASN B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 PHE 389 389 389 PHE PHE B . n 
B 1 390 ILE 390 390 390 ILE ILE B . n 
B 1 391 GLN 391 391 391 GLN GLN B . n 
B 1 392 HIS 392 392 392 HIS HIS B . n 
B 1 393 VAL 393 393 393 VAL VAL B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 SER 395 395 395 SER SER B . n 
B 1 396 ALA 396 396 396 ALA ALA B . n 
B 1 397 VAL 397 397 397 VAL VAL B . n 
B 1 398 PHE 398 398 398 PHE PHE B . n 
B 1 399 ALA 399 399 399 ALA ALA B . n 
B 1 400 VAL 400 400 400 VAL VAL B . n 
B 1 401 PRO 401 401 401 PRO PRO B . n 
B 1 402 PRO 402 402 402 PRO PRO B . n 
B 1 403 GLY 403 403 403 GLY GLY B . n 
B 1 404 VAL 404 404 404 VAL VAL B . n 
B 1 405 ARG 405 405 405 ARG ARG B . n 
B 1 406 ASP 406 406 406 ASP ASP B . n 
B 1 407 ALA 407 407 407 ALA ALA B . n 
B 1 408 ASP 408 408 408 ASP ASP B . n 
B 1 409 ASP 409 409 409 ASP ASP B . n 
B 1 410 TRP 410 410 410 TRP TRP B . n 
B 1 411 TRP 411 411 411 TRP TRP B . n 
B 1 412 GLY 412 412 412 GLY GLY B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 THR 414 414 414 THR THR B . n 
B 1 415 LEU 415 415 415 LEU LEU B . n 
B 1 416 PHE 416 416 416 PHE PHE B . n 
B 1 417 GLY 417 417 417 GLY GLY B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1   501 501 HEM HEM A . 
D 2 HEM 1   501 501 HEM HEM B . 
E 3 HOH 1   601 604 HOH HOH A . 
E 3 HOH 2   602 611 HOH HOH A . 
E 3 HOH 3   603 613 HOH HOH A . 
E 3 HOH 4   604 603 HOH HOH A . 
E 3 HOH 5   605 606 HOH HOH A . 
E 3 HOH 6   606 607 HOH HOH A . 
E 3 HOH 7   607 666 HOH HOH A . 
E 3 HOH 8   608 637 HOH HOH A . 
E 3 HOH 9   609 629 HOH HOH A . 
E 3 HOH 10  610 639 HOH HOH A . 
E 3 HOH 11  611 703 HOH HOH A . 
E 3 HOH 12  612 644 HOH HOH A . 
E 3 HOH 13  613 641 HOH HOH A . 
E 3 HOH 14  614 605 HOH HOH A . 
E 3 HOH 15  615 609 HOH HOH A . 
E 3 HOH 16  616 712 HOH HOH A . 
E 3 HOH 17  617 681 HOH HOH A . 
E 3 HOH 18  618 627 HOH HOH A . 
E 3 HOH 19  619 634 HOH HOH A . 
E 3 HOH 20  620 632 HOH HOH A . 
E 3 HOH 21  621 12  HOH HOH A . 
E 3 HOH 22  622 650 HOH HOH A . 
E 3 HOH 23  623 628 HOH HOH A . 
E 3 HOH 24  624 618 HOH HOH A . 
E 3 HOH 25  625 657 HOH HOH A . 
E 3 HOH 26  626 690 HOH HOH A . 
E 3 HOH 27  627 664 HOH HOH A . 
E 3 HOH 28  628 628 HOH HOH A . 
E 3 HOH 29  629 663 HOH HOH A . 
E 3 HOH 30  630 702 HOH HOH A . 
E 3 HOH 31  631 724 HOH HOH A . 
E 3 HOH 32  632 649 HOH HOH A . 
E 3 HOH 33  633 717 HOH HOH A . 
E 3 HOH 34  634 693 HOH HOH A . 
E 3 HOH 35  635 13  HOH HOH A . 
E 3 HOH 36  636 701 HOH HOH A . 
E 3 HOH 37  637 648 HOH HOH A . 
E 3 HOH 38  638 610 HOH HOH A . 
E 3 HOH 39  639 669 HOH HOH A . 
E 3 HOH 40  640 612 HOH HOH A . 
E 3 HOH 41  641 652 HOH HOH A . 
E 3 HOH 42  642 676 HOH HOH A . 
E 3 HOH 43  643 654 HOH HOH A . 
E 3 HOH 44  644 675 HOH HOH A . 
E 3 HOH 45  645 617 HOH HOH A . 
E 3 HOH 46  646 626 HOH HOH A . 
E 3 HOH 47  647 670 HOH HOH A . 
E 3 HOH 48  648 623 HOH HOH A . 
E 3 HOH 49  649 633 HOH HOH A . 
E 3 HOH 50  650 684 HOH HOH A . 
E 3 HOH 51  651 638 HOH HOH A . 
E 3 HOH 52  652 711 HOH HOH A . 
E 3 HOH 53  653 742 HOH HOH A . 
E 3 HOH 54  654 662 HOH HOH A . 
E 3 HOH 55  655 624 HOH HOH A . 
E 3 HOH 56  656 656 HOH HOH A . 
E 3 HOH 57  657 622 HOH HOH A . 
E 3 HOH 58  658 636 HOH HOH A . 
E 3 HOH 59  659 608 HOH HOH A . 
E 3 HOH 60  660 625 HOH HOH A . 
E 3 HOH 61  661 621 HOH HOH A . 
E 3 HOH 62  662 665 HOH HOH A . 
E 3 HOH 63  663 655 HOH HOH A . 
E 3 HOH 64  664 635 HOH HOH A . 
E 3 HOH 65  665 653 HOH HOH A . 
E 3 HOH 66  666 730 HOH HOH A . 
E 3 HOH 67  667 631 HOH HOH A . 
E 3 HOH 68  668 630 HOH HOH A . 
E 3 HOH 69  669 651 HOH HOH A . 
E 3 HOH 70  670 648 HOH HOH A . 
E 3 HOH 71  671 688 HOH HOH A . 
E 3 HOH 72  672 685 HOH HOH A . 
E 3 HOH 73  673 615 HOH HOH A . 
E 3 HOH 74  674 673 HOH HOH A . 
E 3 HOH 75  675 643 HOH HOH A . 
E 3 HOH 76  676 708 HOH HOH A . 
E 3 HOH 77  677 667 HOH HOH A . 
E 3 HOH 78  678 642 HOH HOH A . 
E 3 HOH 79  679 661 HOH HOH A . 
E 3 HOH 80  680 710 HOH HOH A . 
E 3 HOH 81  681 716 HOH HOH A . 
E 3 HOH 82  682 619 HOH HOH A . 
E 3 HOH 83  683 659 HOH HOH A . 
E 3 HOH 84  684 696 HOH HOH A . 
E 3 HOH 85  685 709 HOH HOH A . 
E 3 HOH 86  686 759 HOH HOH A . 
E 3 HOH 87  687 689 HOH HOH A . 
E 3 HOH 88  688 699 HOH HOH A . 
E 3 HOH 89  689 647 HOH HOH A . 
E 3 HOH 90  690 707 HOH HOH A . 
E 3 HOH 91  691 722 HOH HOH A . 
E 3 HOH 92  692 695 HOH HOH A . 
E 3 HOH 93  693 718 HOH HOH A . 
E 3 HOH 94  694 755 HOH HOH A . 
E 3 HOH 95  695 692 HOH HOH A . 
E 3 HOH 96  696 640 HOH HOH A . 
E 3 HOH 97  697 671 HOH HOH A . 
E 3 HOH 98  698 730 HOH HOH A . 
E 3 HOH 99  699 620 HOH HOH A . 
E 3 HOH 100 700 646 HOH HOH A . 
E 3 HOH 101 701 660 HOH HOH A . 
E 3 HOH 102 702 706 HOH HOH A . 
E 3 HOH 103 703 679 HOH HOH A . 
E 3 HOH 104 704 741 HOH HOH A . 
E 3 HOH 105 705 672 HOH HOH A . 
E 3 HOH 106 706 714 HOH HOH A . 
E 3 HOH 107 707 715 HOH HOH A . 
E 3 HOH 108 708 731 HOH HOH A . 
E 3 HOH 109 709 678 HOH HOH A . 
E 3 HOH 110 710 677 HOH HOH A . 
E 3 HOH 111 711 745 HOH HOH A . 
E 3 HOH 112 712 723 HOH HOH A . 
E 3 HOH 113 713 747 HOH HOH A . 
E 3 HOH 114 714 705 HOH HOH A . 
E 3 HOH 115 715 682 HOH HOH A . 
E 3 HOH 116 716 728 HOH HOH A . 
E 3 HOH 117 717 686 HOH HOH A . 
E 3 HOH 118 718 748 HOH HOH A . 
E 3 HOH 119 719 740 HOH HOH A . 
E 3 HOH 120 720 700 HOH HOH A . 
E 3 HOH 121 721 732 HOH HOH A . 
E 3 HOH 122 722 668 HOH HOH A . 
E 3 HOH 123 723 691 HOH HOH A . 
E 3 HOH 124 724 698 HOH HOH A . 
E 3 HOH 125 725 756 HOH HOH A . 
E 3 HOH 126 726 674 HOH HOH A . 
E 3 HOH 127 727 697 HOH HOH A . 
E 3 HOH 128 728 719 HOH HOH A . 
E 3 HOH 129 729 721 HOH HOH A . 
E 3 HOH 130 730 694 HOH HOH A . 
E 3 HOH 131 731 735 HOH HOH A . 
E 3 HOH 132 732 704 HOH HOH A . 
E 3 HOH 133 733 762 HOH HOH A . 
E 3 HOH 134 734 601 HOH HOH A . 
E 3 HOH 135 735 749 HOH HOH A . 
E 3 HOH 136 736 658 HOH HOH A . 
E 3 HOH 137 737 726 HOH HOH A . 
E 3 HOH 138 738 739 HOH HOH A . 
E 3 HOH 139 739 751 HOH HOH A . 
E 3 HOH 140 740 727 HOH HOH A . 
E 3 HOH 141 741 763 HOH HOH A . 
E 3 HOH 142 742 753 HOH HOH A . 
E 3 HOH 143 743 1   HOH HOH A . 
E 3 HOH 144 744 737 HOH HOH A . 
E 3 HOH 145 745 744 HOH HOH A . 
E 3 HOH 146 746 734 HOH HOH A . 
E 3 HOH 147 747 720 HOH HOH A . 
E 3 HOH 148 748 736 HOH HOH A . 
E 3 HOH 149 749 746 HOH HOH A . 
E 3 HOH 150 750 713 HOH HOH A . 
E 3 HOH 151 751 754 HOH HOH A . 
E 3 HOH 152 752 760 HOH HOH A . 
E 3 HOH 153 753 738 HOH HOH A . 
E 3 HOH 154 754 752 HOH HOH A . 
E 3 HOH 155 755 758 HOH HOH A . 
E 3 HOH 156 756 769 HOH HOH A . 
E 3 HOH 157 757 761 HOH HOH A . 
E 3 HOH 158 758 768 HOH HOH A . 
E 3 HOH 159 759 765 HOH HOH A . 
E 3 HOH 160 760 725 HOH HOH A . 
E 3 HOH 161 761 757 HOH HOH A . 
E 3 HOH 162 762 767 HOH HOH A . 
E 3 HOH 163 763 750 HOH HOH A . 
E 3 HOH 164 764 771 HOH HOH A . 
E 3 HOH 165 765 764 HOH HOH A . 
E 3 HOH 166 766 766 HOH HOH A . 
E 3 HOH 167 767 729 HOH HOH A . 
E 3 HOH 168 768 775 HOH HOH A . 
E 3 HOH 169 769 770 HOH HOH A . 
E 3 HOH 170 770 772 HOH HOH A . 
E 3 HOH 171 771 774 HOH HOH A . 
E 3 HOH 172 772 773 HOH HOH A . 
E 3 HOH 173 773 776 HOH HOH A . 
E 3 HOH 174 774 777 HOH HOH A . 
E 3 HOH 175 775 778 HOH HOH A . 
E 3 HOH 176 776 6   HOH HOH A . 
E 3 HOH 177 777 784 HOH HOH A . 
F 3 HOH 1   601 601 HOH HOH B . 
F 3 HOH 2   602 615 HOH HOH B . 
F 3 HOH 3   603 603 HOH HOH B . 
F 3 HOH 4   604 606 HOH HOH B . 
F 3 HOH 5   605 605 HOH HOH B . 
F 3 HOH 6   606 609 HOH HOH B . 
F 3 HOH 7   607 621 HOH HOH B . 
F 3 HOH 8   608 604 HOH HOH B . 
F 3 HOH 9   609 611 HOH HOH B . 
F 3 HOH 10  610 636 HOH HOH B . 
F 3 HOH 11  611 613 HOH HOH B . 
F 3 HOH 12  612 629 HOH HOH B . 
F 3 HOH 13  613 610 HOH HOH B . 
F 3 HOH 14  614 633 HOH HOH B . 
F 3 HOH 15  615 9   HOH HOH B . 
F 3 HOH 16  616 617 HOH HOH B . 
F 3 HOH 17  617 668 HOH HOH B . 
F 3 HOH 18  618 634 HOH HOH B . 
F 3 HOH 19  619 624 HOH HOH B . 
F 3 HOH 20  620 684 HOH HOH B . 
F 3 HOH 21  621 641 HOH HOH B . 
F 3 HOH 22  622 639 HOH HOH B . 
F 3 HOH 23  623 618 HOH HOH B . 
F 3 HOH 24  624 631 HOH HOH B . 
F 3 HOH 25  625 683 HOH HOH B . 
F 3 HOH 26  626 602 HOH HOH B . 
F 3 HOH 27  627 635 HOH HOH B . 
F 3 HOH 28  628 616 HOH HOH B . 
F 3 HOH 29  629 654 HOH HOH B . 
F 3 HOH 30  630 658 HOH HOH B . 
F 3 HOH 31  631 650 HOH HOH B . 
F 3 HOH 32  632 702 HOH HOH B . 
F 3 HOH 33  633 676 HOH HOH B . 
F 3 HOH 34  634 4   HOH HOH B . 
F 3 HOH 35  635 645 HOH HOH B . 
F 3 HOH 36  636 619 HOH HOH B . 
F 3 HOH 37  637 661 HOH HOH B . 
F 3 HOH 38  638 607 HOH HOH B . 
F 3 HOH 39  639 739 HOH HOH B . 
F 3 HOH 40  640 640 HOH HOH B . 
F 3 HOH 41  641 637 HOH HOH B . 
F 3 HOH 42  642 647 HOH HOH B . 
F 3 HOH 43  643 622 HOH HOH B . 
F 3 HOH 44  644 656 HOH HOH B . 
F 3 HOH 45  645 642 HOH HOH B . 
F 3 HOH 46  646 673 HOH HOH B . 
F 3 HOH 47  647 623 HOH HOH B . 
F 3 HOH 48  648 659 HOH HOH B . 
F 3 HOH 49  649 632 HOH HOH B . 
F 3 HOH 50  650 627 HOH HOH B . 
F 3 HOH 51  651 630 HOH HOH B . 
F 3 HOH 52  652 11  HOH HOH B . 
F 3 HOH 53  653 657 HOH HOH B . 
F 3 HOH 54  654 625 HOH HOH B . 
F 3 HOH 55  655 700 HOH HOH B . 
F 3 HOH 56  656 671 HOH HOH B . 
F 3 HOH 57  657 675 HOH HOH B . 
F 3 HOH 58  658 644 HOH HOH B . 
F 3 HOH 59  659 729 HOH HOH B . 
F 3 HOH 60  660 638 HOH HOH B . 
F 3 HOH 61  661 643 HOH HOH B . 
F 3 HOH 62  662 667 HOH HOH B . 
F 3 HOH 63  663 664 HOH HOH B . 
F 3 HOH 64  664 689 HOH HOH B . 
F 3 HOH 65  665 670 HOH HOH B . 
F 3 HOH 66  666 736 HOH HOH B . 
F 3 HOH 67  667 721 HOH HOH B . 
F 3 HOH 68  668 10  HOH HOH B . 
F 3 HOH 69  669 2   HOH HOH B . 
F 3 HOH 70  670 678 HOH HOH B . 
F 3 HOH 71  671 774 HOH HOH B . 
F 3 HOH 72  672 645 HOH HOH B . 
F 3 HOH 73  673 709 HOH HOH B . 
F 3 HOH 74  674 626 HOH HOH B . 
F 3 HOH 75  675 646 HOH HOH B . 
F 3 HOH 76  676 693 HOH HOH B . 
F 3 HOH 77  677 696 HOH HOH B . 
F 3 HOH 78  678 674 HOH HOH B . 
F 3 HOH 79  679 680 HOH HOH B . 
F 3 HOH 80  680 651 HOH HOH B . 
F 3 HOH 81  681 691 HOH HOH B . 
F 3 HOH 82  682 688 HOH HOH B . 
F 3 HOH 83  683 687 HOH HOH B . 
F 3 HOH 84  684 672 HOH HOH B . 
F 3 HOH 85  685 692 HOH HOH B . 
F 3 HOH 86  686 754 HOH HOH B . 
F 3 HOH 87  687 612 HOH HOH B . 
F 3 HOH 88  688 759 HOH HOH B . 
F 3 HOH 89  689 710 HOH HOH B . 
F 3 HOH 90  690 701 HOH HOH B . 
F 3 HOH 91  691 690 HOH HOH B . 
F 3 HOH 92  692 662 HOH HOH B . 
F 3 HOH 93  693 686 HOH HOH B . 
F 3 HOH 94  694 752 HOH HOH B . 
F 3 HOH 95  695 698 HOH HOH B . 
F 3 HOH 96  696 745 HOH HOH B . 
F 3 HOH 97  697 699 HOH HOH B . 
F 3 HOH 98  698 718 HOH HOH B . 
F 3 HOH 99  699 620 HOH HOH B . 
F 3 HOH 100 700 708 HOH HOH B . 
F 3 HOH 101 701 652 HOH HOH B . 
F 3 HOH 102 702 685 HOH HOH B . 
F 3 HOH 103 703 677 HOH HOH B . 
F 3 HOH 104 704 660 HOH HOH B . 
F 3 HOH 105 705 750 HOH HOH B . 
F 3 HOH 106 706 682 HOH HOH B . 
F 3 HOH 107 707 724 HOH HOH B . 
F 3 HOH 108 708 666 HOH HOH B . 
F 3 HOH 109 709 655 HOH HOH B . 
F 3 HOH 110 710 697 HOH HOH B . 
F 3 HOH 111 711 707 HOH HOH B . 
F 3 HOH 112 712 663 HOH HOH B . 
F 3 HOH 113 713 740 HOH HOH B . 
F 3 HOH 114 714 706 HOH HOH B . 
F 3 HOH 115 715 741 HOH HOH B . 
F 3 HOH 116 716 695 HOH HOH B . 
F 3 HOH 117 717 716 HOH HOH B . 
F 3 HOH 118 718 694 HOH HOH B . 
F 3 HOH 119 719 665 HOH HOH B . 
F 3 HOH 120 720 722 HOH HOH B . 
F 3 HOH 121 721 743 HOH HOH B . 
F 3 HOH 122 722 669 HOH HOH B . 
F 3 HOH 123 723 733 HOH HOH B . 
F 3 HOH 124 724 719 HOH HOH B . 
F 3 HOH 125 725 711 HOH HOH B . 
F 3 HOH 126 726 681 HOH HOH B . 
F 3 HOH 127 727 713 HOH HOH B . 
F 3 HOH 128 728 746 HOH HOH B . 
F 3 HOH 129 729 765 HOH HOH B . 
F 3 HOH 130 730 726 HOH HOH B . 
F 3 HOH 131 731 731 HOH HOH B . 
F 3 HOH 132 732 712 HOH HOH B . 
F 3 HOH 133 733 733 HOH HOH B . 
F 3 HOH 134 734 720 HOH HOH B . 
F 3 HOH 135 735 768 HOH HOH B . 
F 3 HOH 136 736 756 HOH HOH B . 
F 3 HOH 137 737 679 HOH HOH B . 
F 3 HOH 138 738 705 HOH HOH B . 
F 3 HOH 139 739 704 HOH HOH B . 
F 3 HOH 140 740 748 HOH HOH B . 
F 3 HOH 141 741 714 HOH HOH B . 
F 3 HOH 142 742 761 HOH HOH B . 
F 3 HOH 143 743 734 HOH HOH B . 
F 3 HOH 144 744 742 HOH HOH B . 
F 3 HOH 145 745 717 HOH HOH B . 
F 3 HOH 146 746 738 HOH HOH B . 
F 3 HOH 147 747 728 HOH HOH B . 
F 3 HOH 148 748 703 HOH HOH B . 
F 3 HOH 149 749 758 HOH HOH B . 
F 3 HOH 150 750 3   HOH HOH B . 
F 3 HOH 151 751 747 HOH HOH B . 
F 3 HOH 152 752 737 HOH HOH B . 
F 3 HOH 153 753 715 HOH HOH B . 
F 3 HOH 154 754 723 HOH HOH B . 
F 3 HOH 155 755 757 HOH HOH B . 
F 3 HOH 156 756 766 HOH HOH B . 
F 3 HOH 157 757 755 HOH HOH B . 
F 3 HOH 158 758 744 HOH HOH B . 
F 3 HOH 159 759 751 HOH HOH B . 
F 3 HOH 160 760 753 HOH HOH B . 
F 3 HOH 161 761 732 HOH HOH B . 
F 3 HOH 162 762 767 HOH HOH B . 
F 3 HOH 163 763 760 HOH HOH B . 
F 3 HOH 164 764 727 HOH HOH B . 
F 3 HOH 165 765 763 HOH HOH B . 
F 3 HOH 166 766 772 HOH HOH B . 
F 3 HOH 167 767 764 HOH HOH B . 
F 3 HOH 168 768 773 HOH HOH B . 
F 3 HOH 169 769 735 HOH HOH B . 
F 3 HOH 170 770 777 HOH HOH B . 
F 3 HOH 171 771 769 HOH HOH B . 
F 3 HOH 172 772 770 HOH HOH B . 
F 3 HOH 173 773 725 HOH HOH B . 
F 3 HOH 174 774 749 HOH HOH B . 
F 3 HOH 175 775 776 HOH HOH B . 
F 3 HOH 176 776 771 HOH HOH B . 
F 3 HOH 177 777 762 HOH HOH B . 
F 3 HOH 178 778 779 HOH HOH B . 
F 3 HOH 179 779 780 HOH HOH B . 
F 3 HOH 180 780 778 HOH HOH B . 
F 3 HOH 181 781 782 HOH HOH B . 
F 3 HOH 182 782 7   HOH HOH B . 
F 3 HOH 183 783 781 HOH HOH B . 
F 3 HOH 184 784 783 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 134 ? CE  ? A LYS 134 CE  
2  1 Y 1 A LYS 134 ? NZ  ? A LYS 134 NZ  
3  1 Y 1 A LYS 167 ? CG  ? A LYS 167 CG  
4  1 Y 1 A LYS 167 ? CD  ? A LYS 167 CD  
5  1 Y 1 A LYS 167 ? CE  ? A LYS 167 CE  
6  1 Y 1 A LYS 167 ? NZ  ? A LYS 167 NZ  
7  1 Y 1 A ARG 175 ? CD  ? A ARG 175 CD  
8  1 Y 1 A ARG 175 ? NE  ? A ARG 175 NE  
9  1 Y 1 A ARG 175 ? CZ  ? A ARG 175 CZ  
10 1 Y 1 A ARG 175 ? NH1 ? A ARG 175 NH1 
11 1 Y 1 A ARG 175 ? NH2 ? A ARG 175 NH2 
12 1 Y 1 A LYS 228 ? CE  ? A LYS 228 CE  
13 1 Y 1 A LYS 228 ? NZ  ? A LYS 228 NZ  
14 1 Y 1 A LYS 249 ? CG  ? A LYS 249 CG  
15 1 Y 1 A LYS 249 ? CD  ? A LYS 249 CD  
16 1 Y 1 A LYS 249 ? CE  ? A LYS 249 CE  
17 1 Y 1 A LYS 249 ? NZ  ? A LYS 249 NZ  
18 1 Y 1 A ASP 250 ? CG  ? A ASP 250 CG  
19 1 Y 1 A ASP 250 ? OD1 ? A ASP 250 OD1 
20 1 Y 1 A ASP 250 ? OD2 ? A ASP 250 OD2 
21 1 Y 1 A ARG 254 ? NE  ? A ARG 254 NE  
22 1 Y 1 A ARG 254 ? CZ  ? A ARG 254 CZ  
23 1 Y 1 A ARG 254 ? NH1 ? A ARG 254 NH1 
24 1 Y 1 A ARG 254 ? NH2 ? A ARG 254 NH2 
25 1 Y 1 A LYS 261 ? CD  ? A LYS 261 CD  
26 1 Y 1 A LYS 261 ? CE  ? A LYS 261 CE  
27 1 Y 1 A LYS 261 ? NZ  ? A LYS 261 NZ  
28 1 Y 1 A GLU 292 ? OE2 ? A GLU 292 OE2 
29 1 Y 1 A LYS 319 ? CD  ? A LYS 319 CD  
30 1 Y 1 A LYS 319 ? CE  ? A LYS 319 CE  
31 1 Y 1 A LYS 319 ? NZ  ? A LYS 319 NZ  
32 1 Y 1 A LYS 322 ? NZ  ? A LYS 322 NZ  
33 1 Y 1 A ARG 405 ? CD  ? A ARG 405 CD  
34 1 Y 1 A ARG 405 ? NE  ? A ARG 405 NE  
35 1 Y 1 A ARG 405 ? CZ  ? A ARG 405 CZ  
36 1 Y 1 A ARG 405 ? NH1 ? A ARG 405 NH1 
37 1 Y 1 A ARG 405 ? NH2 ? A ARG 405 NH2 
38 1 Y 1 B GLU 113 ? OE2 ? B GLU 113 OE2 
39 1 Y 1 B LEU 119 ? CG  ? B LEU 119 CG  
40 1 Y 1 B LEU 119 ? CD1 ? B LEU 119 CD1 
41 1 Y 1 B LEU 119 ? CD2 ? B LEU 119 CD2 
42 1 Y 1 B LYS 134 ? CE  ? B LYS 134 CE  
43 1 Y 1 B LYS 134 ? NZ  ? B LYS 134 NZ  
44 1 Y 1 B LYS 167 ? CG  ? B LYS 167 CG  
45 1 Y 1 B LYS 167 ? CD  ? B LYS 167 CD  
46 1 Y 1 B LYS 167 ? CE  ? B LYS 167 CE  
47 1 Y 1 B LYS 167 ? NZ  ? B LYS 167 NZ  
48 1 Y 1 B ARG 175 ? CD  ? B ARG 175 CD  
49 1 Y 1 B ARG 175 ? NE  ? B ARG 175 NE  
50 1 Y 1 B ARG 175 ? CZ  ? B ARG 175 CZ  
51 1 Y 1 B ARG 175 ? NH1 ? B ARG 175 NH1 
52 1 Y 1 B ARG 175 ? NH2 ? B ARG 175 NH2 
53 1 Y 1 B LYS 228 ? CD  ? B LYS 228 CD  
54 1 Y 1 B LYS 228 ? CE  ? B LYS 228 CE  
55 1 Y 1 B LYS 228 ? NZ  ? B LYS 228 NZ  
56 1 Y 1 B LYS 249 ? CD  ? B LYS 249 CD  
57 1 Y 1 B LYS 249 ? CE  ? B LYS 249 CE  
58 1 Y 1 B LYS 249 ? NZ  ? B LYS 249 NZ  
59 1 Y 1 B GLU 260 ? CD  ? B GLU 260 CD  
60 1 Y 1 B GLU 260 ? OE1 ? B GLU 260 OE1 
61 1 Y 1 B GLU 260 ? OE2 ? B GLU 260 OE2 
62 1 Y 1 B LYS 261 ? CE  ? B LYS 261 CE  
63 1 Y 1 B LYS 261 ? NZ  ? B LYS 261 NZ  
64 1 Y 1 B ARG 287 ? CZ  ? B ARG 287 CZ  
65 1 Y 1 B ARG 287 ? NH1 ? B ARG 287 NH1 
66 1 Y 1 B ARG 287 ? NH2 ? B ARG 287 NH2 
67 1 Y 1 B LYS 311 ? CD  ? B LYS 311 CD  
68 1 Y 1 B LYS 311 ? CE  ? B LYS 311 CE  
69 1 Y 1 B LYS 311 ? NZ  ? B LYS 311 NZ  
70 1 Y 1 B LYS 322 ? NZ  ? B LYS 322 NZ  
71 1 Y 1 B ARG 356 ? NE  ? B ARG 356 NE  
72 1 Y 1 B ARG 356 ? CZ  ? B ARG 356 CZ  
73 1 Y 1 B ARG 356 ? NH1 ? B ARG 356 NH1 
74 1 Y 1 B ARG 356 ? NH2 ? B ARG 356 NH2 
75 1 Y 1 B ARG 405 ? CZ  ? B ARG 405 CZ  
76 1 Y 1 B ARG 405 ? NH1 ? B ARG 405 NH1 
77 1 Y 1 B ARG 405 ? NH2 ? B ARG 405 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0352 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8PXQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.567 
_cell.length_a_esd                 ? 
_cell.length_b                     68.140 
_cell.length_b_esd                 ? 
_cell.length_c                     74.800 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8PXQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8PXQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1:1 v/v ratio of a solution containing 6.2 mg/ml Y389F DtpAa in 20 mM sodium phosphate, 150 mM NaCl pH 7 with a precipitant solution consisting of 100 mM HEPES pH 7 and 15% PEG 6000 to give a final volume of 400 ul.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX225-HS' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.13 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL2 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8PXQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.7 
_reflns.d_resolution_low                               48.85 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     73582 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                70.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.13 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.879 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   0.279 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.7 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5386 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.514 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  0.753 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.28 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.06 
_refine.aniso_B[2][2]                            -0.37 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.11 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.050 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8PXQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             48.85 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     73582 
_refine.ls_number_reflns_R_free                  3803 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16880 
_refine.ls_R_factor_R_free                       0.20502 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16695 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.100 
_refine.pdbx_overall_ESU_R_Free                  0.101 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.667 
_refine.overall_SU_ML                            0.085 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        48.85 
_refine_hist.number_atoms_solvent             361 
_refine_hist.number_atoms_total               5914 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5510 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.014  0.012  5746  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  5073  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.924  1.668  7847  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.649  1.570  11751 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.740  5.000  732   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.383 10.000 54    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.690 10.000 792   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.097  0.200  826   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  6882  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  1255  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.240  1.801  2919  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.219  1.800  2918  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.927  2.696  3654  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.929  2.697  3655  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.339  2.077  2827  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.340  2.077  2825  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.779  2.991  4193  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.225  23.049 6279  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.217  22.998 6256  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             297 
_refine_ls_shell.number_reflns_R_work             5386 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.257 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.303 
# 
_struct.entry_id                     8PXQ 
_struct.title                        'SFX Ferric structure of Y389F variant of A type dye-decolourising peroxidase DtpAa' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8PXQ 
_struct_keywords.text            'Heme peroxidase, dye-decolourising peroxidase, ferric, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A7U9DT46_STRLI 
_struct_ref.pdbx_db_accession          A0A7U9DT46 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDTDSPAPAPSPSRRSLIGWGGAGLALGAAAAAGGAVAMDRAGADADPAGADAGSAVPFHGAHQAGIATPVQDRLHFAA
FDVTTEDRAAFVALLKEWTAAARRLTAGHAVGEGAYGGLPEAPPDDTGEALGLKPSRLTLTIGFGPSLFTRFGLADLRPE
ALADLPKFPGDNLDRARSGGDLCVQACADDPQVAVHAIRNLARIGFGKVVVRWSQLGFGKTSSTTPDKQTPRNLLGFKDG
TRNIAGTEKDRLDRFVWAAEKDGTPWMTGGSYLVARRIRMHIETWDRASLQEQEDVFGRDKGEGAPVGKAKERDEPFLKA
MKPDAHVRLAHPDSNGGATLLRRGYSFTDGTDGLGRLDAGLFFLAYQRDIRTGFVPVQRNLATDALNEYIQHVGSAVFAV
PPGVRDADDWWGSTLFG
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8PXQ A 1 ? 417 ? A0A7U9DT46 1 ? 417 ? 1 417 
2 1 8PXQ B 1 ? 417 ? A0A7U9DT46 1 ? 417 ? 1 417 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8PXQ PHE A 389 ? UNP A0A7U9DT46 TYR 389 'engineered mutation' 389 1 
2 8PXQ PHE B 389 ? UNP A0A7U9DT46 TYR 389 'engineered mutation' 389 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7000  ? 
1 MORE         -63   ? 
1 'SSA (A^2)'  25980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 87  ? ALA A 107 ? ASP A 87  ALA A 107 1 ? 21 
HELX_P HELX_P2  AA2 PRO A 146 ? ARG A 151 ? PRO A 146 ARG A 151 5 ? 6  
HELX_P HELX_P3  AA3 LEU A 154 ? ARG A 158 ? LEU A 154 ARG A 158 5 ? 5  
HELX_P HELX_P4  AA4 ASP A 174 ? SER A 178 ? ASP A 174 SER A 178 5 ? 5  
HELX_P HELX_P5  AA5 ASP A 190 ? GLY A 205 ? ASP A 190 GLY A 205 1 ? 16 
HELX_P HELX_P6  AA6 GLU A 248 ? VAL A 256 ? GLU A 248 VAL A 256 1 ? 9  
HELX_P HELX_P7  AA7 ALA A 259 ? GLY A 263 ? ALA A 259 GLY A 263 5 ? 5  
HELX_P HELX_P8  AA8 THR A 264 ? THR A 268 ? THR A 264 THR A 268 5 ? 5  
HELX_P HELX_P9  AA9 HIS A 281 ? ARG A 287 ? HIS A 281 ARG A 287 1 ? 7  
HELX_P HELX_P10 AB1 SER A 289 ? GLY A 298 ? SER A 289 GLY A 298 1 ? 10 
HELX_P HELX_P11 AB2 PHE A 317 ? MET A 321 ? PHE A 317 MET A 321 5 ? 5  
HELX_P HELX_P12 AB3 ALA A 325 ? HIS A 331 ? ALA A 325 HIS A 331 1 ? 7  
HELX_P HELX_P13 AB4 PRO A 332 ? ASN A 335 ? PRO A 332 ASN A 335 5 ? 4  
HELX_P HELX_P14 AB5 ASP A 369 ? THR A 372 ? ASP A 369 THR A 372 5 ? 4  
HELX_P HELX_P15 AB6 GLY A 373 ? LEU A 381 ? GLY A 373 LEU A 381 1 ? 9  
HELX_P HELX_P16 AB7 ALA A 382 ? GLU A 388 ? ALA A 382 GLU A 388 5 ? 7  
HELX_P HELX_P17 AB8 ASP B 87  ? ALA B 107 ? ASP B 87  ALA B 107 1 ? 21 
HELX_P HELX_P18 AB9 PRO B 146 ? ARG B 151 ? PRO B 146 ARG B 151 5 ? 6  
HELX_P HELX_P19 AC1 LEU B 154 ? ARG B 158 ? LEU B 154 ARG B 158 5 ? 5  
HELX_P HELX_P20 AC2 ASP B 174 ? SER B 178 ? ASP B 174 SER B 178 5 ? 5  
HELX_P HELX_P21 AC3 ASP B 190 ? GLY B 205 ? ASP B 190 GLY B 205 1 ? 16 
HELX_P HELX_P22 AC4 GLU B 248 ? VAL B 256 ? GLU B 248 VAL B 256 1 ? 9  
HELX_P HELX_P23 AC5 ALA B 259 ? GLY B 263 ? ALA B 259 GLY B 263 5 ? 5  
HELX_P HELX_P24 AC6 THR B 264 ? THR B 268 ? THR B 264 THR B 268 5 ? 5  
HELX_P HELX_P25 AC7 HIS B 281 ? ARG B 287 ? HIS B 281 ARG B 287 1 ? 7  
HELX_P HELX_P26 AC8 SER B 289 ? GLY B 298 ? SER B 289 GLY B 298 1 ? 10 
HELX_P HELX_P27 AC9 PHE B 317 ? MET B 321 ? PHE B 317 MET B 321 5 ? 5  
HELX_P HELX_P28 AD1 ALA B 325 ? HIS B 331 ? ALA B 325 HIS B 331 1 ? 7  
HELX_P HELX_P29 AD2 PRO B 332 ? ASN B 335 ? PRO B 332 ASN B 335 5 ? 4  
HELX_P HELX_P30 AD3 ASP B 369 ? THR B 372 ? ASP B 369 THR B 372 5 ? 4  
HELX_P HELX_P31 AD4 GLY B 373 ? LEU B 381 ? GLY B 373 LEU B 381 1 ? 9  
HELX_P HELX_P32 AD5 ALA B 382 ? GLU B 388 ? ALA B 382 GLU B 388 5 ? 7  
HELX_P HELX_P33 AD6 GLY B 412 ? GLY B 417 ? GLY B 412 GLY B 417 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 326 NE2 ? ? ? 1_555 C HEM . FE ? ? A HIS 326 A HEM 501 1_555 ? ? ? ? ? ? ? 2.143 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 E HOH . O  ? ? A HEM 501 A HOH 700 1_555 ? ? ? ? ? ? ? 2.403 ? ? 
metalc3 metalc ? ? B HIS 326 NE2 ? ? ? 1_555 D HEM . FE ? ? B HIS 326 B HEM 501 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc4 metalc ? ? D HEM .   FE  ? ? ? 1_555 F HOH . O  ? ? B HEM 501 B HOH 634 1_555 ? ? ? ? ? ? ? 2.686 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 326 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 90.5  ? 
2  NE2 ? A HIS 326 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 93.3  ? 
3  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.1  ? 
4  NE2 ? A HIS 326 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 96.2  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 173.2 ? 
6  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 90.2  ? 
7  NE2 ? A HIS 326 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 96.0  ? 
8  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 91.7  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 170.7 ? 
10 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 88.9  ? 
11 NE2 ? A HIS 326 ? A HIS 326 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 700 ? 1_555 169.2 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 700 ? 1_555 81.8  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 700 ? 1_555 79.0  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 700 ? 1_555 91.5  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 O  ? E HOH . ? A HOH 700 ? 1_555 91.8  ? 
16 NE2 ? B HIS 326 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NA ? D HEM . ? B HEM 501 ? 1_555 94.6  ? 
17 NE2 ? B HIS 326 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NB ? D HEM . ? B HEM 501 ? 1_555 96.1  ? 
18 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NB ? D HEM . ? B HEM 501 ? 1_555 89.1  ? 
19 NE2 ? B HIS 326 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 98.9  ? 
20 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 166.5 ? 
21 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 NC ? D HEM . ? B HEM 501 ? 1_555 88.5  ? 
22 NE2 ? B HIS 326 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 99.5  ? 
23 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 87.8  ? 
24 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 164.3 ? 
25 NC  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 ND ? D HEM . ? B HEM 501 ? 1_555 91.0  ? 
26 NE2 ? B HIS 326 ? B HIS 326 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  ? F HOH . ? B HOH 634 ? 1_555 167.7 ? 
27 NA  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  ? F HOH . ? B HOH 634 ? 1_555 77.0  ? 
28 NB  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  ? F HOH . ? B HOH 634 ? 1_555 75.0  ? 
29 NC  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  ? F HOH . ? B HOH 634 ? 1_555 89.6  ? 
30 ND  ? D HEM .   ? B HEM 501 ? 1_555 FE ? D HEM . ? B HEM 501 ? 1_555 O  ? F HOH . ? B HOH 634 ? 1_555 89.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 139 ? PHE A 144 ? THR A 139 PHE A 144 
AA1 2 LEU A 182 ? ALA A 188 ? LEU A 182 ALA A 188 
AA1 3 ARG A 75  ? VAL A 83  ? ARG A 75  VAL A 83  
AA1 4 VAL A 209 ? GLY A 217 ? VAL A 209 GLY A 217 
AA2 1 GLY A 219 ? LYS A 220 ? GLY A 219 LYS A 220 
AA2 2 TYR A 345 ? PHE A 347 ? TYR A 345 PHE A 347 
AA2 3 GLY A 360 ? GLN A 367 ? GLY A 360 GLN A 367 
AA2 4 LEU A 341 ? ARG A 342 ? LEU A 341 ARG A 342 
AA3 1 GLY A 219 ? LYS A 220 ? GLY A 219 LYS A 220 
AA3 2 TYR A 345 ? PHE A 347 ? TYR A 345 PHE A 347 
AA3 3 GLY A 360 ? GLN A 367 ? GLY A 360 GLN A 367 
AA3 4 SER A 271 ? MET A 280 ? SER A 271 MET A 280 
AA3 5 ILE A 390 ? VAL A 400 ? ILE A 390 VAL A 400 
AA4 1 THR B 139 ? PHE B 144 ? THR B 139 PHE B 144 
AA4 2 LEU B 182 ? ALA B 188 ? LEU B 182 ALA B 188 
AA4 3 ARG B 75  ? VAL B 83  ? ARG B 75  VAL B 83  
AA4 4 VAL B 209 ? PHE B 218 ? VAL B 209 PHE B 218 
AA5 1 LEU B 341 ? ARG B 342 ? LEU B 341 ARG B 342 
AA5 2 LEU B 357 ? GLN B 367 ? LEU B 357 GLN B 367 
AA5 3 TYR B 345 ? THR B 351 ? TYR B 345 THR B 351 
AA6 1 LEU B 341 ? ARG B 342 ? LEU B 341 ARG B 342 
AA6 2 LEU B 357 ? GLN B 367 ? LEU B 357 GLN B 367 
AA6 3 SER B 271 ? MET B 280 ? SER B 271 MET B 280 
AA6 4 ILE B 390 ? VAL B 400 ? ILE B 390 VAL B 400 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 141 ? N THR A 141 O GLN A 185 ? O GLN A 185 
AA1 2 3 O LEU A 182 ? O LEU A 182 N PHE A 81  ? N PHE A 81  
AA1 3 4 N PHE A 78  ? N PHE A 78  O GLN A 215 ? O GLN A 215 
AA2 1 2 N GLY A 219 ? N GLY A 219 O SER A 346 ? O SER A 346 
AA2 2 3 N TYR A 345 ? N TYR A 345 O PHE A 362 ? O PHE A 362 
AA2 3 4 O TYR A 366 ? O TYR A 366 N LEU A 341 ? N LEU A 341 
AA3 1 2 N GLY A 219 ? N GLY A 219 O SER A 346 ? O SER A 346 
AA3 2 3 N TYR A 345 ? N TYR A 345 O PHE A 362 ? O PHE A 362 
AA3 3 4 O PHE A 363 ? O PHE A 363 N ARG A 276 ? N ARG A 276 
AA3 4 5 N LEU A 273 ? N LEU A 273 O PHE A 398 ? O PHE A 398 
AA4 1 2 N THR B 141 ? N THR B 141 O GLN B 185 ? O GLN B 185 
AA4 2 3 O LEU B 182 ? O LEU B 182 N PHE B 81  ? N PHE B 81  
AA4 3 4 N ALA B 80  ? N ALA B 80  O TRP B 213 ? O TRP B 213 
AA5 1 2 N LEU B 341 ? N LEU B 341 O TYR B 366 ? O TYR B 366 
AA5 2 3 O PHE B 362 ? O PHE B 362 N TYR B 345 ? N TYR B 345 
AA6 1 2 N LEU B 341 ? N LEU B 341 O TYR B 366 ? O TYR B 366 
AA6 2 3 O ALA B 359 ? O ALA B 359 N MET B 280 ? N MET B 280 
AA6 3 4 N LEU B 273 ? N LEU B 273 O PHE B 398 ? O PHE B 398 
# 
_pdbx_entry_details.entry_id                   8PXQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    97 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.07 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 NE A ARG 75  ? B CZ A ARG 75  ? B NH2 A ARG 75  ? B 115.63 120.30 -4.67 0.50 N 
2  1 NE A ARG 88  ? ? CZ A ARG 88  ? ? NH2 A ARG 88  ? ? 116.77 120.30 -3.53 0.50 N 
3  1 NE A ARG 199 ? ? CZ A ARG 199 ? ? NH1 A ARG 199 ? ? 116.89 120.30 -3.41 0.50 N 
4  1 NE A ARG 251 ? ? CZ A ARG 251 ? ? NH1 A ARG 251 ? ? 123.37 120.30 3.07  0.50 N 
5  1 NE A ARG 251 ? ? CZ A ARG 251 ? ? NH2 A ARG 251 ? ? 115.78 120.30 -4.52 0.50 N 
6  1 NE A ARG 299 ? ? CZ A ARG 299 ? ? NH1 A ARG 299 ? ? 123.90 120.30 3.60  0.50 N 
7  1 NE A ARG 299 ? ? CZ A ARG 299 ? ? NH2 A ARG 299 ? ? 116.13 120.30 -4.17 0.50 N 
8  1 NE A ARG 342 ? ? CZ A ARG 342 ? ? NH2 A ARG 342 ? ? 116.05 120.30 -4.25 0.50 N 
9  1 NE B ARG 75  ? ? CZ B ARG 75  ? ? NH2 B ARG 75  ? ? 117.19 120.30 -3.11 0.50 N 
10 1 NE B ARG 251 ? ? CZ B ARG 251 ? ? NH2 B ARG 251 ? ? 117.17 120.30 -3.13 0.50 N 
11 1 NE B ARG 276 ? ? CZ B ARG 276 ? ? NH2 B ARG 276 ? ? 116.79 120.30 -3.51 0.50 N 
12 1 NE B ARG 342 ? ? CZ B ARG 342 ? ? NH1 B ARG 342 ? ? 124.50 120.30 4.20  0.50 N 
13 1 NE B ARG 342 ? ? CZ B ARG 342 ? ? NH2 B ARG 342 ? ? 115.45 120.30 -4.85 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 68  ? ? -120.68 -69.46  
2 1 ARG A 242 ? ? -105.17 79.21   
3 1 ASN A 243 ? ? -118.29 -158.06 
4 1 ARG A 343 ? ? -146.72 36.87   
5 1 ASP A 349 ? ? -118.15 55.59   
6 1 VAL B 256 ? ? -120.34 -54.13  
7 1 ARG B 343 ? ? -144.82 35.35   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1  1 ARG A 75  ? A 0.134 'SIDE CHAIN' 
2  1 ARG A 88  ? ? 0.250 'SIDE CHAIN' 
3  1 ARG A 104 ? ? 0.084 'SIDE CHAIN' 
4  1 ARG A 151 ? ? 0.099 'SIDE CHAIN' 
5  1 ARG A 177 ? ? 0.176 'SIDE CHAIN' 
6  1 ARG A 242 ? ? 0.094 'SIDE CHAIN' 
7  1 ARG A 279 ? ? 0.077 'SIDE CHAIN' 
8  1 ARG A 379 ? ? 0.155 'SIDE CHAIN' 
9  1 ARG B 104 ? ? 0.090 'SIDE CHAIN' 
10 1 ARG B 151 ? ? 0.123 'SIDE CHAIN' 
11 1 ARG B 177 ? ? 0.106 'SIDE CHAIN' 
12 1 ARG B 242 ? ? 0.091 'SIDE CHAIN' 
13 1 ARG B 251 ? ? 0.123 'SIDE CHAIN' 
14 1 ARG B 254 ? ? 0.092 'SIDE CHAIN' 
15 1 ARG B 279 ? ? 0.108 'SIDE CHAIN' 
16 1 ARG B 313 ? ? 0.084 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A THR 2   ? A THR 2   
3   1 Y 1 A ASP 3   ? A ASP 3   
4   1 Y 1 A THR 4   ? A THR 4   
5   1 Y 1 A ASP 5   ? A ASP 5   
6   1 Y 1 A SER 6   ? A SER 6   
7   1 Y 1 A PRO 7   ? A PRO 7   
8   1 Y 1 A ALA 8   ? A ALA 8   
9   1 Y 1 A PRO 9   ? A PRO 9   
10  1 Y 1 A ALA 10  ? A ALA 10  
11  1 Y 1 A PRO 11  ? A PRO 11  
12  1 Y 1 A SER 12  ? A SER 12  
13  1 Y 1 A PRO 13  ? A PRO 13  
14  1 Y 1 A SER 14  ? A SER 14  
15  1 Y 1 A ARG 15  ? A ARG 15  
16  1 Y 1 A ARG 16  ? A ARG 16  
17  1 Y 1 A SER 17  ? A SER 17  
18  1 Y 1 A LEU 18  ? A LEU 18  
19  1 Y 1 A ILE 19  ? A ILE 19  
20  1 Y 1 A GLY 20  ? A GLY 20  
21  1 Y 1 A TRP 21  ? A TRP 21  
22  1 Y 1 A GLY 22  ? A GLY 22  
23  1 Y 1 A GLY 23  ? A GLY 23  
24  1 Y 1 A ALA 24  ? A ALA 24  
25  1 Y 1 A GLY 25  ? A GLY 25  
26  1 Y 1 A LEU 26  ? A LEU 26  
27  1 Y 1 A ALA 27  ? A ALA 27  
28  1 Y 1 A LEU 28  ? A LEU 28  
29  1 Y 1 A GLY 29  ? A GLY 29  
30  1 Y 1 A ALA 30  ? A ALA 30  
31  1 Y 1 A ALA 31  ? A ALA 31  
32  1 Y 1 A ALA 32  ? A ALA 32  
33  1 Y 1 A ALA 33  ? A ALA 33  
34  1 Y 1 A ALA 34  ? A ALA 34  
35  1 Y 1 A GLY 35  ? A GLY 35  
36  1 Y 1 A GLY 36  ? A GLY 36  
37  1 Y 1 A ALA 37  ? A ALA 37  
38  1 Y 1 A VAL 38  ? A VAL 38  
39  1 Y 1 A ALA 39  ? A ALA 39  
40  1 Y 1 A MET 40  ? A MET 40  
41  1 Y 1 A ASP 41  ? A ASP 41  
42  1 Y 1 A ARG 42  ? A ARG 42  
43  1 Y 1 A ALA 43  ? A ALA 43  
44  1 Y 1 A GLY 44  ? A GLY 44  
45  1 Y 1 A ALA 45  ? A ALA 45  
46  1 Y 1 A ASP 46  ? A ASP 46  
47  1 Y 1 A ALA 47  ? A ALA 47  
48  1 Y 1 A ASP 48  ? A ASP 48  
49  1 Y 1 A PRO 49  ? A PRO 49  
50  1 Y 1 A ALA 50  ? A ALA 50  
51  1 Y 1 A GLY 51  ? A GLY 51  
52  1 Y 1 A ALA 52  ? A ALA 52  
53  1 Y 1 A ASP 53  ? A ASP 53  
54  1 Y 1 A ALA 54  ? A ALA 54  
55  1 Y 1 A GLY 417 ? A GLY 417 
56  1 Y 1 B MET 1   ? B MET 1   
57  1 Y 1 B THR 2   ? B THR 2   
58  1 Y 1 B ASP 3   ? B ASP 3   
59  1 Y 1 B THR 4   ? B THR 4   
60  1 Y 1 B ASP 5   ? B ASP 5   
61  1 Y 1 B SER 6   ? B SER 6   
62  1 Y 1 B PRO 7   ? B PRO 7   
63  1 Y 1 B ALA 8   ? B ALA 8   
64  1 Y 1 B PRO 9   ? B PRO 9   
65  1 Y 1 B ALA 10  ? B ALA 10  
66  1 Y 1 B PRO 11  ? B PRO 11  
67  1 Y 1 B SER 12  ? B SER 12  
68  1 Y 1 B PRO 13  ? B PRO 13  
69  1 Y 1 B SER 14  ? B SER 14  
70  1 Y 1 B ARG 15  ? B ARG 15  
71  1 Y 1 B ARG 16  ? B ARG 16  
72  1 Y 1 B SER 17  ? B SER 17  
73  1 Y 1 B LEU 18  ? B LEU 18  
74  1 Y 1 B ILE 19  ? B ILE 19  
75  1 Y 1 B GLY 20  ? B GLY 20  
76  1 Y 1 B TRP 21  ? B TRP 21  
77  1 Y 1 B GLY 22  ? B GLY 22  
78  1 Y 1 B GLY 23  ? B GLY 23  
79  1 Y 1 B ALA 24  ? B ALA 24  
80  1 Y 1 B GLY 25  ? B GLY 25  
81  1 Y 1 B LEU 26  ? B LEU 26  
82  1 Y 1 B ALA 27  ? B ALA 27  
83  1 Y 1 B LEU 28  ? B LEU 28  
84  1 Y 1 B GLY 29  ? B GLY 29  
85  1 Y 1 B ALA 30  ? B ALA 30  
86  1 Y 1 B ALA 31  ? B ALA 31  
87  1 Y 1 B ALA 32  ? B ALA 32  
88  1 Y 1 B ALA 33  ? B ALA 33  
89  1 Y 1 B ALA 34  ? B ALA 34  
90  1 Y 1 B GLY 35  ? B GLY 35  
91  1 Y 1 B GLY 36  ? B GLY 36  
92  1 Y 1 B ALA 37  ? B ALA 37  
93  1 Y 1 B VAL 38  ? B VAL 38  
94  1 Y 1 B ALA 39  ? B ALA 39  
95  1 Y 1 B MET 40  ? B MET 40  
96  1 Y 1 B ASP 41  ? B ASP 41  
97  1 Y 1 B ARG 42  ? B ARG 42  
98  1 Y 1 B ALA 43  ? B ALA 43  
99  1 Y 1 B GLY 44  ? B GLY 44  
100 1 Y 1 B ALA 45  ? B ALA 45  
101 1 Y 1 B ASP 46  ? B ASP 46  
102 1 Y 1 B ALA 47  ? B ALA 47  
103 1 Y 1 B ASP 48  ? B ASP 48  
104 1 Y 1 B PRO 49  ? B PRO 49  
105 1 Y 1 B ALA 50  ? B ALA 50  
106 1 Y 1 B GLY 51  ? B GLY 51  
107 1 Y 1 B ALA 52  ? B ALA 52  
108 1 Y 1 B ASP 53  ? B ASP 53  
109 1 Y 1 B ALA 54  ? B ALA 54  
110 1 Y 1 B GLY 55  ? B GLY 55  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
PHE N    N  N N 325 
PHE CA   C  N S 326 
PHE C    C  N N 327 
PHE O    O  N N 328 
PHE CB   C  N N 329 
PHE CG   C  Y N 330 
PHE CD1  C  Y N 331 
PHE CD2  C  Y N 332 
PHE CE1  C  Y N 333 
PHE CE2  C  Y N 334 
PHE CZ   C  Y N 335 
PHE OXT  O  N N 336 
PHE H    H  N N 337 
PHE H2   H  N N 338 
PHE HA   H  N N 339 
PHE HB2  H  N N 340 
PHE HB3  H  N N 341 
PHE HD1  H  N N 342 
PHE HD2  H  N N 343 
PHE HE1  H  N N 344 
PHE HE2  H  N N 345 
PHE HZ   H  N N 346 
PHE HXT  H  N N 347 
PRO N    N  N N 348 
PRO CA   C  N S 349 
PRO C    C  N N 350 
PRO O    O  N N 351 
PRO CB   C  N N 352 
PRO CG   C  N N 353 
PRO CD   C  N N 354 
PRO OXT  O  N N 355 
PRO H    H  N N 356 
PRO HA   H  N N 357 
PRO HB2  H  N N 358 
PRO HB3  H  N N 359 
PRO HG2  H  N N 360 
PRO HG3  H  N N 361 
PRO HD2  H  N N 362 
PRO HD3  H  N N 363 
PRO HXT  H  N N 364 
SER N    N  N N 365 
SER CA   C  N S 366 
SER C    C  N N 367 
SER O    O  N N 368 
SER CB   C  N N 369 
SER OG   O  N N 370 
SER OXT  O  N N 371 
SER H    H  N N 372 
SER H2   H  N N 373 
SER HA   H  N N 374 
SER HB2  H  N N 375 
SER HB3  H  N N 376 
SER HG   H  N N 377 
SER HXT  H  N N 378 
THR N    N  N N 379 
THR CA   C  N S 380 
THR C    C  N N 381 
THR O    O  N N 382 
THR CB   C  N R 383 
THR OG1  O  N N 384 
THR CG2  C  N N 385 
THR OXT  O  N N 386 
THR H    H  N N 387 
THR H2   H  N N 388 
THR HA   H  N N 389 
THR HB   H  N N 390 
THR HG1  H  N N 391 
THR HG21 H  N N 392 
THR HG22 H  N N 393 
THR HG23 H  N N 394 
THR HXT  H  N N 395 
TRP N    N  N N 396 
TRP CA   C  N S 397 
TRP C    C  N N 398 
TRP O    O  N N 399 
TRP CB   C  N N 400 
TRP CG   C  Y N 401 
TRP CD1  C  Y N 402 
TRP CD2  C  Y N 403 
TRP NE1  N  Y N 404 
TRP CE2  C  Y N 405 
TRP CE3  C  Y N 406 
TRP CZ2  C  Y N 407 
TRP CZ3  C  Y N 408 
TRP CH2  C  Y N 409 
TRP OXT  O  N N 410 
TRP H    H  N N 411 
TRP H2   H  N N 412 
TRP HA   H  N N 413 
TRP HB2  H  N N 414 
TRP HB3  H  N N 415 
TRP HD1  H  N N 416 
TRP HE1  H  N N 417 
TRP HE3  H  N N 418 
TRP HZ2  H  N N 419 
TRP HZ3  H  N N 420 
TRP HH2  H  N N 421 
TRP HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/R021015/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6I43 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_data_reduction.crystal_hits          11101 
_pdbx_serial_crystallography_data_reduction.diffrn_id             1 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frame_hits            11101 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        ? 
_pdbx_serial_crystallography_data_reduction.frames_total          49955 
_pdbx_serial_crystallography_data_reduction.lattices_indexed      ? 
_pdbx_serial_crystallography_data_reduction.lattices_merged       ? 
_pdbx_serial_crystallography_data_reduction.xfel_pulse_events     ? 
_pdbx_serial_crystallography_data_reduction.xfel_run_numbers      ? 
# 
_pdbx_serial_crystallography_measurement.collection_time_total        0.25 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.focal_spot_size              ? 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.pulse_duration               10 
_pdbx_serial_crystallography_measurement.pulse_energy                 360 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          11 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   30 
# 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               25600 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.details                         ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   mylar 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  'Silicon chip' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_horizontal             ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_vertical               ? 
# 
_atom_sites.entry_id                    8PXQ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.013780 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003822 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014676 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.013874 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 55  ? 17.143  -18.240 23.372  1.00 34.19 ? 55  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 55  ? 18.105  -17.958 24.461  1.00 32.56 ? 55  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 55  ? 19.559  -18.264 24.081  1.00 31.42 ? 55  GLY A C   1 
ATOM   4    O  O   . GLY A 1 55  ? 20.470  -17.729 24.708  1.00 27.01 ? 55  GLY A O   1 
ATOM   5    N  N   . SER A 1 56  ? 19.776  -19.091 23.039  1.00 32.31 ? 56  SER A N   1 
ATOM   6    C  CA  . SER A 1 56  ? 21.065  -19.709 22.747  1.00 30.84 ? 56  SER A CA  1 
ATOM   7    C  C   . SER A 1 56  ? 22.058  -18.693 22.174  1.00 27.02 ? 56  SER A C   1 
ATOM   8    O  O   . SER A 1 56  ? 21.710  -17.589 21.759  1.00 25.38 ? 56  SER A O   1 
ATOM   9    C  CB  . SER A 1 56  ? 20.858  -20.889 21.821  1.00 31.86 ? 56  SER A CB  1 
ATOM   10   O  OG  . SER A 1 56  ? 20.261  -20.446 20.597  1.00 36.77 ? 56  SER A OG  1 
ATOM   11   N  N   . ALA A 1 57  ? 23.360  -19.028 22.249  1.00 26.67 ? 57  ALA A N   1 
ATOM   12   C  CA  . ALA A 1 57  ? 24.408  -18.228 21.656  1.00 23.23 ? 57  ALA A CA  1 
ATOM   13   C  C   . ALA A 1 57  ? 24.527  -18.560 20.163  1.00 24.40 ? 57  ALA A C   1 
ATOM   14   O  O   . ALA A 1 57  ? 24.302  -19.663 19.667  1.00 24.90 ? 57  ALA A O   1 
ATOM   15   C  CB  . ALA A 1 57  ? 25.715  -18.438 22.388  1.00 22.13 ? 57  ALA A CB  1 
ATOM   16   N  N   . VAL A 1 58  ? 24.848  -17.533 19.393  1.00 16.15 ? 58  VAL A N   1 
ATOM   17   C  CA  . VAL A 1 58  ? 25.243  -17.653 18.019  1.00 17.11 ? 58  VAL A CA  1 
ATOM   18   C  C   . VAL A 1 58  ? 26.763  -17.555 18.040  1.00 15.49 ? 58  VAL A C   1 
ATOM   19   O  O   . VAL A 1 58  ? 27.363  -16.624 18.588  1.00 15.48 ? 58  VAL A O   1 
ATOM   20   C  CB  . VAL A 1 58  ? 24.615  -16.543 17.160  1.00 19.31 ? 58  VAL A CB  1 
ATOM   21   C  CG1 . VAL A 1 58  ? 25.177  -16.580 15.756  1.00 20.33 ? 58  VAL A CG1 1 
ATOM   22   C  CG2 . VAL A 1 58  ? 23.106  -16.637 17.154  1.00 19.57 ? 58  VAL A CG2 1 
ATOM   23   N  N   . PRO A 1 59  ? 27.440  -18.532 17.398  1.00 18.32 ? 59  PRO A N   1 
ATOM   24   C  CA  . PRO A 1 59  ? 28.895  -18.522 17.354  1.00 18.70 ? 59  PRO A CA  1 
ATOM   25   C  C   . PRO A 1 59  ? 29.415  -17.226 16.743  1.00 17.60 ? 59  PRO A C   1 
ATOM   26   O  O   . PRO A 1 59  ? 28.940  -16.793 15.689  1.00 16.12 ? 59  PRO A O   1 
ATOM   27   C  CB  . PRO A 1 59  ? 29.232  -19.800 16.532  1.00 20.97 ? 59  PRO A CB  1 
ATOM   28   C  CG  . PRO A 1 59  ? 27.996  -20.667 16.581  1.00 21.21 ? 59  PRO A CG  1 
ATOM   29   C  CD  . PRO A 1 59  ? 26.831  -19.713 16.760  1.00 21.13 ? 59  PRO A CD  1 
ATOM   30   N  N   . PHE A 1 60  ? 30.435  -16.641 17.402  1.00 14.78 ? 60  PHE A N   1 
ATOM   31   C  CA  . PHE A 1 60  ? 30.999  -15.365 17.028  1.00 14.81 ? 60  PHE A CA  1 
ATOM   32   C  C   . PHE A 1 60  ? 31.981  -15.511 15.860  1.00 14.77 ? 60  PHE A C   1 
ATOM   33   O  O   . PHE A 1 60  ? 32.107  -14.634 14.981  1.00 14.58 ? 60  PHE A O   1 
ATOM   34   C  CB  . PHE A 1 60  ? 31.571  -14.674 18.263  1.00 16.60 ? 60  PHE A CB  1 
ATOM   35   C  CG  . PHE A 1 60  ? 32.267  -13.365 18.005  1.00 16.51 ? 60  PHE A CG  1 
ATOM   36   C  CD1 . PHE A 1 60  ? 31.526  -12.241 17.662  1.00 17.72 ? 60  PHE A CD1 1 
ATOM   37   C  CD2 . PHE A 1 60  ? 33.651  -13.273 17.977  1.00 16.80 ? 60  PHE A CD2 1 
ATOM   38   C  CE1 . PHE A 1 60  ? 32.156  -11.057 17.308  1.00 16.56 ? 60  PHE A CE1 1 
ATOM   39   C  CE2 . PHE A 1 60  ? 34.266  -12.068 17.632  1.00 17.12 ? 60  PHE A CE2 1 
ATOM   40   C  CZ  . PHE A 1 60  ? 33.517  -10.954 17.347  1.00 16.38 ? 60  PHE A CZ  1 
ATOM   41   N  N   . HIS A 1 61  ? 32.789  -16.574 15.926  1.00 16.36 ? 61  HIS A N   1 
ATOM   42   C  CA  . HIS A 1 61  ? 33.851  -16.812 14.972  1.00 17.06 ? 61  HIS A CA  1 
ATOM   43   C  C   . HIS A 1 61  ? 33.304  -17.472 13.715  1.00 14.86 ? 61  HIS A C   1 
ATOM   44   O  O   . HIS A 1 61  ? 32.329  -18.241 13.737  1.00 15.92 ? 61  HIS A O   1 
ATOM   45   C  CB  . HIS A 1 61  ? 34.913  -17.715 15.605  1.00 16.47 ? 61  HIS A CB  1 
ATOM   46   C  CG  . HIS A 1 61  ? 35.618  -17.098 16.789  1.00 17.20 ? 61  HIS A CG  1 
ATOM   47   N  ND1 . HIS A 1 61  ? 36.086  -17.897 17.834  1.00 20.01 ? 61  HIS A ND1 1 
ATOM   48   C  CD2 . HIS A 1 61  ? 36.085  -15.847 17.045  1.00 19.17 ? 61  HIS A CD2 1 
ATOM   49   C  CE1 . HIS A 1 61  ? 36.783  -17.139 18.682  1.00 20.63 ? 61  HIS A CE1 1 
ATOM   50   N  NE2 . HIS A 1 61  ? 36.786  -15.861 18.216  1.00 17.80 ? 61  HIS A NE2 1 
ATOM   51   N  N   . GLY A 1 62  ? 33.995  -17.199 12.605  1.00 16.70 ? 62  GLY A N   1 
ATOM   52   C  CA  . GLY A 1 62  ? 33.710  -17.867 11.355  1.00 17.24 ? 62  GLY A CA  1 
ATOM   53   C  C   . GLY A 1 62  ? 34.439  -17.161 10.223  1.00 16.15 ? 62  GLY A C   1 
ATOM   54   O  O   . GLY A 1 62  ? 35.041  -16.081 10.400  1.00 17.71 ? 62  GLY A O   1 
ATOM   55   N  N   . ALA A 1 63  ? 34.244  -17.683 9.019   1.00 16.49 ? 63  ALA A N   1 
ATOM   56   C  CA  . ALA A 1 63  ? 34.771  -17.063 7.816   1.00 19.58 ? 63  ALA A CA  1 
ATOM   57   C  C   . ALA A 1 63  ? 34.022  -15.767 7.515   1.00 16.64 ? 63  ALA A C   1 
ATOM   58   O  O   . ALA A 1 63  ? 34.529  -14.864 6.901   1.00 16.06 ? 63  ALA A O   1 
ATOM   59   C  CB  . ALA A 1 63  ? 34.558  -18.065 6.684   1.00 21.39 ? 63  ALA A CB  1 
ATOM   60   N  N   . HIS A 1 64  ? 32.760  -15.726 7.912   1.00 15.48 ? 64  HIS A N   1 
ATOM   61   C  CA  . HIS A 1 64  ? 31.935  -14.554 7.774   1.00 16.71 ? 64  HIS A CA  1 
ATOM   62   C  C   . HIS A 1 64  ? 31.543  -14.066 9.171   1.00 16.68 ? 64  HIS A C   1 
ATOM   63   O  O   . HIS A 1 64  ? 31.436  -14.846 10.135  1.00 15.71 ? 64  HIS A O   1 
ATOM   64   C  CB  . HIS A 1 64  ? 30.646  -14.858 7.006   1.00 18.17 ? 64  HIS A CB  1 
ATOM   65   C  CG  . HIS A 1 64  ? 30.877  -15.547 5.696   1.00 18.87 ? 64  HIS A CG  1 
ATOM   66   N  ND1 . HIS A 1 64  ? 31.678  -15.067 4.681   1.00 18.31 ? 64  HIS A ND1 1 
ATOM   67   C  CD2 . HIS A 1 64  ? 30.524  -16.821 5.379   1.00 21.17 ? 64  HIS A CD2 1 
ATOM   68   C  CE1 . HIS A 1 64  ? 31.747  -15.999 3.744   1.00 21.52 ? 64  HIS A CE1 1 
ATOM   69   N  NE2 . HIS A 1 64  ? 31.073  -17.075 4.163   1.00 20.32 ? 64  HIS A NE2 1 
ATOM   70   N  N   . GLN A 1 65  ? 31.172  -12.775 9.249   1.00 15.24 ? 65  GLN A N   1 
ATOM   71   C  CA  . GLN A 1 65  ? 30.571  -12.296 10.473  1.00 14.18 ? 65  GLN A CA  1 
ATOM   72   C  C   . GLN A 1 65  ? 29.170  -12.869 10.582  1.00 13.48 ? 65  GLN A C   1 
ATOM   73   O  O   . GLN A 1 65  ? 28.459  -12.965 9.626   1.00 13.24 ? 65  GLN A O   1 
ATOM   74   C  CB  . GLN A 1 65  ? 30.514  -10.742 10.463  1.00 15.41 ? 65  GLN A CB  1 
ATOM   75   C  CG  . GLN A 1 65  ? 31.881  -10.070 10.612  1.00 16.06 ? 65  GLN A CG  1 
ATOM   76   C  CD  . GLN A 1 65  ? 31.732  -8.578  10.838  1.00 13.55 ? 65  GLN A CD  1 
ATOM   77   O  OE1 . GLN A 1 65  ? 31.226  -8.158  11.884  1.00 14.30 ? 65  GLN A OE1 1 
ATOM   78   N  NE2 . GLN A 1 65  ? 32.144  -7.807  9.849   1.00 13.23 ? 65  GLN A NE2 1 
ATOM   79   N  N   . ALA A 1 66  ? 28.739  -13.116 11.814  1.00 14.03 ? 66  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 66  ? 27.370  -13.458 12.125  1.00 14.24 ? 66  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 66  ? 26.531  -12.167 12.020  1.00 14.54 ? 66  ALA A C   1 
ATOM   82   O  O   . ALA A 1 66  ? 27.074  -11.075 11.954  1.00 18.76 ? 66  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 66  ? 27.262  -14.065 13.508  1.00 16.00 ? 66  ALA A CB  1 
ATOM   84   N  N   . GLY A 1 67  ? 25.213  -12.354 11.926  1.00 14.13 ? 67  GLY A N   1 
ATOM   85   C  CA  . GLY A 1 67  ? 24.265  -11.259 11.900  1.00 13.73 ? 67  GLY A CA  1 
ATOM   86   C  C   . GLY A 1 67  ? 23.912  -10.851 10.491  1.00 14.68 ? 67  GLY A C   1 
ATOM   87   O  O   . GLY A 1 67  ? 23.217  -9.873  10.324  1.00 14.41 ? 67  GLY A O   1 
ATOM   88   N  N   . ILE A 1 68  ? 24.224  -11.701 9.509   1.00 13.56 ? 68  ILE A N   1 
ATOM   89   C  CA  . ILE A 1 68  ? 23.899  -11.482 8.092   1.00 14.73 ? 68  ILE A CA  1 
ATOM   90   C  C   . ILE A 1 68  ? 23.023  -12.629 7.596   1.00 14.19 ? 68  ILE A C   1 
ATOM   91   O  O   . ILE A 1 68  ? 21.778  -12.486 7.471   1.00 13.49 ? 68  ILE A O   1 
ATOM   92   C  CB  . ILE A 1 68  ? 25.160  -11.281 7.222   1.00 15.41 ? 68  ILE A CB  1 
ATOM   93   C  CG1 . ILE A 1 68  ? 26.016  -10.190 7.898   1.00 18.93 ? 68  ILE A CG1 1 
ATOM   94   C  CG2 . ILE A 1 68  ? 24.773  -10.973 5.761   1.00 15.20 ? 68  ILE A CG2 1 
ATOM   95   C  CD1 . ILE A 1 68  ? 27.386  -9.957  7.331   1.00 20.84 ? 68  ILE A CD1 1 
ATOM   96   N  N   . ALA A 1 69  ? 23.637  -13.826 7.491   1.00 14.23 ? 69  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 69  ? 22.954  -15.035 7.075   1.00 17.05 ? 69  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 69  ? 22.173  -15.666 8.250   1.00 17.60 ? 69  ALA A C   1 
ATOM   99   O  O   . ALA A 1 69  ? 21.304  -16.488 7.996   1.00 17.80 ? 69  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 69  ? 23.937  -16.085 6.502   1.00 17.97 ? 69  ALA A CB  1 
ATOM   101  N  N   . THR A 1 70  ? 22.600  -15.347 9.502   1.00 15.76 ? 70  THR A N   1 
ATOM   102  C  CA  . THR A 1 70  ? 22.014  -15.753 10.772  1.00 15.48 ? 70  THR A CA  1 
ATOM   103  C  C   . THR A 1 70  ? 20.512  -15.532 10.746  1.00 14.40 ? 70  THR A C   1 
ATOM   104  O  O   . THR A 1 70  ? 20.103  -14.510 10.159  1.00 13.40 ? 70  THR A O   1 
ATOM   105  C  CB  . THR A 1 70  ? 22.537  -14.853 11.903  1.00 17.69 ? 70  THR A CB  1 
ATOM   106  O  OG1 . THR A 1 70  ? 23.945  -14.912 11.797  1.00 18.60 ? 70  THR A OG1 1 
ATOM   107  C  CG2 . THR A 1 70  ? 22.117  -15.317 13.296  1.00 20.20 ? 70  THR A CG2 1 
ATOM   108  N  N   . PRO A 1 71  ? 19.682  -16.452 11.309  1.00 13.38 ? 71  PRO A N   1 
ATOM   109  C  CA  . PRO A 1 71  ? 18.261  -16.187 11.551  1.00 14.13 ? 71  PRO A CA  1 
ATOM   110  C  C   . PRO A 1 71  ? 18.058  -14.830 12.191  1.00 12.87 ? 71  PRO A C   1 
ATOM   111  O  O   . PRO A 1 71  ? 18.823  -14.398 13.078  1.00 12.51 ? 71  PRO A O   1 
ATOM   112  C  CB  . PRO A 1 71  ? 17.795  -17.331 12.506  1.00 15.43 ? 71  PRO A CB  1 
ATOM   113  C  CG  . PRO A 1 71  ? 18.756  -18.459 12.164  1.00 16.86 ? 71  PRO A CG  1 
ATOM   114  C  CD  . PRO A 1 71  ? 20.060  -17.807 11.754  1.00 15.76 ? 71  PRO A CD  1 
ATOM   115  N  N   . VAL A 1 72  ? 17.076  -14.100 11.641  1.00 13.04 ? 72  VAL A N   1 
ATOM   116  C  CA  . VAL A 1 72  ? 16.838  -12.732 12.031  1.00 11.88 ? 72  VAL A CA  1 
ATOM   117  C  C   . VAL A 1 72  ? 16.253  -12.720 13.441  1.00 11.64 ? 72  VAL A C   1 
ATOM   118  O  O   . VAL A 1 72  ? 15.175  -13.323 13.689  1.00 13.44 ? 72  VAL A O   1 
ATOM   119  C  CB  . VAL A 1 72  ? 15.907  -12.041 11.006  1.00 13.64 ? 72  VAL A CB  1 
ATOM   120  C  CG1 . VAL A 1 72  ? 15.673  -10.614 11.440  1.00 13.06 ? 72  VAL A CG1 1 
ATOM   121  C  CG2 . VAL A 1 72  ? 16.485  -12.116 9.590   1.00 11.88 ? 72  VAL A CG2 1 
ATOM   122  N  N   . GLN A 1 73  ? 16.925  -11.971 14.314  1.00 12.42 ? 73  GLN A N   1 
ATOM   123  C  CA  . GLN A 1 73  ? 16.547  -11.883 15.719  1.00 12.94 ? 73  GLN A CA  1 
ATOM   124  C  C   . GLN A 1 73  ? 15.479  -10.818 15.890  1.00 14.38 ? 73  GLN A C   1 
ATOM   125  O  O   . GLN A 1 73  ? 15.261  -9.968  15.011  1.00 12.89 ? 73  GLN A O   1 
ATOM   126  C  CB  . GLN A 1 73  ? 17.758  -11.639 16.651  1.00 13.30 ? 73  GLN A CB  1 
ATOM   127  C  CG  . GLN A 1 73  ? 18.920  -12.586 16.374  1.00 13.51 ? 73  GLN A CG  1 
ATOM   128  C  CD  . GLN A 1 73  ? 19.999  -12.025 15.454  1.00 13.32 ? 73  GLN A CD  1 
ATOM   129  O  OE1 . GLN A 1 73  ? 19.652  -11.508 14.375  1.00 13.80 ? 73  GLN A OE1 1 
ATOM   130  N  NE2 . GLN A 1 73  ? 21.289  -12.125 15.846  1.00 12.63 ? 73  GLN A NE2 1 
ATOM   131  N  N   . ASP A 1 74  ? 14.807  -10.844 17.038  1.00 15.31 ? 74  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 74  ? 13.628  -9.964  17.191  1.00 15.10 ? 74  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 74  ? 13.947  -8.493  17.265  1.00 14.30 ? 74  ASP A C   1 
ATOM   134  O  O   . ASP A 1 74  ? 13.068  -7.647  17.003  1.00 17.30 ? 74  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 74  ? 12.856  -10.345 18.472  1.00 17.84 ? 74  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 74  ? 12.132  -11.677 18.343  1.00 24.48 ? 74  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 74  ? 11.914  -12.116 17.244  1.00 25.26 ? 74  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 74  ? 11.792  -12.258 19.375  1.00 28.86 ? 74  ASP A OD2 1 
ATOM   139  N  N   A ARG A 1 75  ? 15.115  -8.135  17.797  0.60 14.38 ? 75  ARG A N   1 
ATOM   140  N  N   B ARG A 1 75  ? 15.130  -8.140  17.773  0.40 15.57 ? 75  ARG A N   1 
ATOM   141  C  CA  A ARG A 1 75  ? 15.410  -6.752  18.091  0.60 13.94 ? 75  ARG A CA  1 
ATOM   142  C  CA  B ARG A 1 75  ? 15.411  -6.767  18.142  0.40 15.58 ? 75  ARG A CA  1 
ATOM   143  C  C   A ARG A 1 75  ? 16.702  -6.280  17.458  0.60 14.68 ? 75  ARG A C   1 
ATOM   144  C  C   B ARG A 1 75  ? 16.698  -6.278  17.489  0.40 15.54 ? 75  ARG A C   1 
ATOM   145  O  O   A ARG A 1 75  ? 17.644  -7.055  17.277  0.60 16.86 ? 75  ARG A O   1 
ATOM   146  O  O   B ARG A 1 75  ? 17.629  -7.061  17.287  0.40 17.62 ? 75  ARG A O   1 
ATOM   147  C  CB  A ARG A 1 75  ? 15.518  -6.552  19.602  0.60 14.89 ? 75  ARG A CB  1 
ATOM   148  C  CB  B ARG A 1 75  ? 15.528  -6.672  19.666  0.40 17.28 ? 75  ARG A CB  1 
ATOM   149  C  CG  A ARG A 1 75  ? 14.234  -6.888  20.343  0.60 16.16 ? 75  ARG A CG  1 
ATOM   150  C  CG  B ARG A 1 75  ? 14.637  -7.640  20.446  0.40 18.91 ? 75  ARG A CG  1 
ATOM   151  C  CD  A ARG A 1 75  ? 13.071  -5.916  20.120  0.60 16.66 ? 75  ARG A CD  1 
ATOM   152  C  CD  B ARG A 1 75  ? 13.227  -7.159  20.680  0.40 20.50 ? 75  ARG A CD  1 
ATOM   153  N  NE  A ARG A 1 75  ? 13.395  -4.583  20.614  0.60 18.13 ? 75  ARG A NE  1 
ATOM   154  N  NE  B ARG A 1 75  ? 12.253  -7.701  19.798  0.40 19.59 ? 75  ARG A NE  1 
ATOM   155  C  CZ  A ARG A 1 75  ? 12.597  -3.827  21.368  0.60 18.01 ? 75  ARG A CZ  1 
ATOM   156  C  CZ  B ARG A 1 75  ? 10.986  -7.922  20.103  0.40 15.76 ? 75  ARG A CZ  1 
ATOM   157  N  NH1 A ARG A 1 75  ? 11.485  -4.357  21.885  0.60 17.62 ? 75  ARG A NH1 1 
ATOM   158  N  NH1 B ARG A 1 75  ? 10.618  -7.975  21.385  0.40 15.99 ? 75  ARG A NH1 1 
ATOM   159  N  NH2 A ARG A 1 75  ? 12.962  -2.574  21.611  0.60 20.63 ? 75  ARG A NH2 1 
ATOM   160  N  NH2 B ARG A 1 75  ? 10.131  -7.826  19.099  0.40 11.26 ? 75  ARG A NH2 1 
ATOM   161  N  N   . LEU A 1 76  ? 16.754  -4.961  17.220  1.00 13.14 ? 76  LEU A N   1 
ATOM   162  C  CA  . LEU A 1 76  ? 17.923  -4.318  16.651  1.00 13.53 ? 76  LEU A CA  1 
ATOM   163  C  C   . LEU A 1 76  ? 18.297  -3.116  17.496  1.00 14.81 ? 76  LEU A C   1 
ATOM   164  O  O   . LEU A 1 76  ? 17.426  -2.299  17.856  1.00 14.36 ? 76  LEU A O   1 
ATOM   165  C  CB  . LEU A 1 76  ? 17.626  -3.885  15.208  1.00 15.20 ? 76  LEU A CB  1 
ATOM   166  C  CG  . LEU A 1 76  ? 18.657  -2.979  14.555  1.00 13.24 ? 76  LEU A CG  1 
ATOM   167  C  CD1 . LEU A 1 76  ? 19.899  -3.765  14.172  1.00 16.93 ? 76  LEU A CD1 1 
ATOM   168  C  CD2 . LEU A 1 76  ? 18.074  -2.257  13.331  1.00 15.42 ? 76  LEU A CD2 1 
ATOM   169  N  N   . HIS A 1 77  ? 19.607  -2.941  17.653  1.00 12.42 ? 77  HIS A N   1 
ATOM   170  C  CA  . HIS A 1 77  ? 20.161  -1.660  18.029  1.00 13.14 ? 77  HIS A CA  1 
ATOM   171  C  C   . HIS A 1 77  ? 21.351  -1.404  17.126  1.00 15.40 ? 77  HIS A C   1 
ATOM   172  O  O   . HIS A 1 77  ? 22.338  -2.141  17.172  1.00 15.15 ? 77  HIS A O   1 
ATOM   173  C  CB  . HIS A 1 77  ? 20.537  -1.623  19.521  1.00 16.28 ? 77  HIS A CB  1 
ATOM   174  C  CG  . HIS A 1 77  ? 20.885  -0.275  20.066  1.00 19.67 ? 77  HIS A CG  1 
ATOM   175  N  ND1 . HIS A 1 77  ? 20.892  -0.045  21.416  1.00 25.51 ? 77  HIS A ND1 1 
ATOM   176  C  CD2 . HIS A 1 77  ? 21.288  0.876   19.472  1.00 24.55 ? 77  HIS A CD2 1 
ATOM   177  C  CE1 . HIS A 1 77  ? 21.285  1.206   21.623  1.00 26.42 ? 77  HIS A CE1 1 
ATOM   178  N  NE2 . HIS A 1 77  ? 21.506  1.812   20.450  1.00 24.90 ? 77  HIS A NE2 1 
ATOM   179  N  N   . PHE A 1 78  ? 21.195  -0.420  16.245  1.00 12.85 ? 78  PHE A N   1 
ATOM   180  C  CA  . PHE A 1 78  ? 22.190  -0.115  15.240  1.00 12.98 ? 78  PHE A CA  1 
ATOM   181  C  C   . PHE A 1 78  ? 22.825  1.210   15.628  1.00 14.66 ? 78  PHE A C   1 
ATOM   182  O  O   . PHE A 1 78  ? 22.132  2.163   15.918  1.00 17.42 ? 78  PHE A O   1 
ATOM   183  C  CB  . PHE A 1 78  ? 21.514  0.002   13.873  1.00 13.79 ? 78  PHE A CB  1 
ATOM   184  C  CG  . PHE A 1 78  ? 22.448  0.053   12.687  1.00 13.80 ? 78  PHE A CG  1 
ATOM   185  C  CD1 . PHE A 1 78  ? 23.132  1.221   12.357  1.00 15.77 ? 78  PHE A CD1 1 
ATOM   186  C  CD2 . PHE A 1 78  ? 22.684  -1.091  11.948  1.00 13.97 ? 78  PHE A CD2 1 
ATOM   187  C  CE1 . PHE A 1 78  ? 24.034  1.219   11.289  1.00 14.10 ? 78  PHE A CE1 1 
ATOM   188  C  CE2 . PHE A 1 78  ? 23.501  -1.044  10.842  1.00 16.04 ? 78  PHE A CE2 1 
ATOM   189  C  CZ  . PHE A 1 78  ? 24.186  0.093   10.539  1.00 16.54 ? 78  PHE A CZ  1 
ATOM   190  N  N   . ALA A 1 79  ? 24.135  1.261   15.707  1.00 13.19 ? 79  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 79  ? 24.787  2.522   15.956  1.00 15.99 ? 79  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 79  ? 25.829  2.779   14.872  1.00 17.30 ? 79  ALA A C   1 
ATOM   193  O  O   . ALA A 1 79  ? 26.571  1.896   14.487  1.00 17.03 ? 79  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 79  ? 25.407  2.496   17.331  1.00 17.04 ? 79  ALA A CB  1 
ATOM   195  N  N   . ALA A 1 80  ? 25.913  4.045   14.432  1.00 15.66 ? 80  ALA A N   1 
ATOM   196  C  CA  . ALA A 1 80  ? 26.965  4.513   13.574  1.00 17.42 ? 80  ALA A CA  1 
ATOM   197  C  C   . ALA A 1 80  ? 27.875  5.377   14.452  1.00 16.95 ? 80  ALA A C   1 
ATOM   198  O  O   . ALA A 1 80  ? 27.388  6.202   15.248  1.00 19.18 ? 80  ALA A O   1 
ATOM   199  C  CB  . ALA A 1 80  ? 26.426  5.353   12.396  1.00 17.97 ? 80  ALA A CB  1 
ATOM   200  N  N   . PHE A 1 81  ? 29.184  5.217   14.253  1.00 17.18 ? 81  PHE A N   1 
ATOM   201  C  CA  . PHE A 1 81  ? 30.173  5.937   15.032  1.00 17.43 ? 81  PHE A CA  1 
ATOM   202  C  C   . PHE A 1 81  ? 31.051  6.738   14.080  1.00 17.86 ? 81  PHE A C   1 
ATOM   203  O  O   . PHE A 1 81  ? 31.292  6.336   12.966  1.00 18.37 ? 81  PHE A O   1 
ATOM   204  C  CB  . PHE A 1 81  ? 31.099  5.028   15.845  1.00 16.41 ? 81  PHE A CB  1 
ATOM   205  C  CG  . PHE A 1 81  ? 30.448  4.131   16.850  1.00 16.83 ? 81  PHE A CG  1 
ATOM   206  C  CD1 . PHE A 1 81  ? 29.828  2.958   16.473  1.00 20.45 ? 81  PHE A CD1 1 
ATOM   207  C  CD2 . PHE A 1 81  ? 30.563  4.404   18.209  1.00 22.80 ? 81  PHE A CD2 1 
ATOM   208  C  CE1 . PHE A 1 81  ? 29.293  2.111   17.442  1.00 22.62 ? 81  PHE A CE1 1 
ATOM   209  C  CE2 . PHE A 1 81  ? 29.946  3.608   19.170  1.00 25.57 ? 81  PHE A CE2 1 
ATOM   210  C  CZ  . PHE A 1 81  ? 29.374  2.433   18.784  1.00 24.07 ? 81  PHE A CZ  1 
ATOM   211  N  N   . ASP A 1 82  ? 31.489  7.921   14.542  1.00 19.36 ? 82  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 82  ? 32.618  8.606   13.912  1.00 20.95 ? 82  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 82  ? 33.900  8.401   14.729  1.00 20.64 ? 82  ASP A C   1 
ATOM   214  O  O   . ASP A 1 82  ? 33.851  8.246   15.942  1.00 20.47 ? 82  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 82  ? 32.300  10.095  13.720  1.00 22.34 ? 82  ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 82  ? 31.236  10.315  12.640  1.00 21.90 ? 82  ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 82  ? 31.123  9.486   11.701  1.00 20.62 ? 82  ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 82  ? 30.565  11.343  12.693  1.00 22.12 ? 82  ASP A OD2 1 
ATOM   219  N  N   . VAL A 1 83  ? 35.032  8.414   14.027  1.00 19.51 ? 83  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 83  ? 36.317  8.199   14.642  1.00 22.16 ? 83  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 83  ? 36.882  9.585   14.992  1.00 25.11 ? 83  VAL A C   1 
ATOM   222  O  O   . VAL A 1 83  ? 36.788  10.494  14.184  1.00 21.52 ? 83  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 83  ? 37.221  7.406   13.689  1.00 23.27 ? 83  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 83  ? 38.645  7.317   14.248  1.00 23.72 ? 83  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 83  ? 36.617  6.011   13.445  1.00 24.92 ? 83  VAL A CG2 1 
ATOM   226  N  N   . THR A 1 84  ? 37.407  9.712   16.207  1.00 23.36 ? 84  THR A N   1 
ATOM   227  C  CA  . THR A 1 84  ? 37.936  10.974  16.714  1.00 25.74 ? 84  THR A CA  1 
ATOM   228  C  C   . THR A 1 84  ? 39.441  10.909  16.956  1.00 32.19 ? 84  THR A C   1 
ATOM   229  O  O   . THR A 1 84  ? 39.998  11.934  17.290  1.00 39.90 ? 84  THR A O   1 
ATOM   230  C  CB  . THR A 1 84  ? 37.215  11.397  17.996  1.00 26.65 ? 84  THR A CB  1 
ATOM   231  O  OG1 . THR A 1 84  ? 37.366  10.385  18.972  1.00 26.06 ? 84  THR A OG1 1 
ATOM   232  C  CG2 . THR A 1 84  ? 35.728  11.607  17.821  1.00 25.68 ? 84  THR A CG2 1 
ATOM   233  N  N   . THR A 1 85  ? 40.105  9.765   16.760  1.00 27.25 ? 85  THR A N   1 
ATOM   234  C  CA  . THR A 1 85  ? 41.549  9.675   16.900  1.00 26.69 ? 85  THR A CA  1 
ATOM   235  C  C   . THR A 1 85  ? 42.167  9.719   15.510  1.00 31.45 ? 85  THR A C   1 
ATOM   236  O  O   . THR A 1 85  ? 41.585  9.201   14.562  1.00 26.46 ? 85  THR A O   1 
ATOM   237  C  CB  . THR A 1 85  ? 41.952  8.404   17.680  1.00 31.90 ? 85  THR A CB  1 
ATOM   238  O  OG1 . THR A 1 85  ? 43.388  8.346   17.758  1.00 25.80 ? 85  THR A OG1 1 
ATOM   239  C  CG2 . THR A 1 85  ? 41.477  7.107   17.058  1.00 31.80 ? 85  THR A CG2 1 
ATOM   240  N  N   . GLU A 1 86  ? 43.381  10.298  15.383  1.00 28.87 ? 86  GLU A N   1 
ATOM   241  C  CA  . GLU A 1 86  ? 44.158  10.198  14.171  1.00 30.24 ? 86  GLU A CA  1 
ATOM   242  C  C   . GLU A 1 86  ? 45.279  9.186   14.288  1.00 31.10 ? 86  GLU A C   1 
ATOM   243  O  O   . GLU A 1 86  ? 45.985  8.996   13.299  1.00 32.77 ? 86  GLU A O   1 
ATOM   244  C  CB  . GLU A 1 86  ? 44.756  11.544  13.730  1.00 39.06 ? 86  GLU A CB  1 
ATOM   245  C  CG  . GLU A 1 86  ? 43.741  12.423  12.988  1.00 47.56 ? 86  GLU A CG  1 
ATOM   246  C  CD  . GLU A 1 86  ? 44.016  13.910  13.170  1.00 61.43 ? 86  GLU A CD  1 
ATOM   247  O  OE1 . GLU A 1 86  ? 45.208  14.288  13.008  1.00 56.03 ? 86  GLU A OE1 1 
ATOM   248  O  OE2 . GLU A 1 86  ? 43.067  14.679  13.536  1.00 61.26 ? 86  GLU A OE2 1 
ATOM   249  N  N   . ASP A 1 87  ? 45.401  8.519   15.449  1.00 26.03 ? 87  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 87  ? 46.462  7.567   15.721  1.00 25.76 ? 87  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 87  ? 45.990  6.177   15.305  1.00 26.39 ? 87  ASP A C   1 
ATOM   252  O  O   . ASP A 1 87  ? 45.115  5.615   15.947  1.00 23.59 ? 87  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 87  ? 46.842  7.649   17.198  1.00 26.29 ? 87  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 87  ? 47.929  6.700   17.686  1.00 30.00 ? 87  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 87  ? 48.344  5.777   16.976  1.00 31.96 ? 87  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 87  ? 48.281  6.877   18.859  1.00 30.21 ? 87  ASP A OD2 1 
ATOM   257  N  N   . ARG A 1 88  ? 46.626  5.654   14.260  1.00 24.56 ? 88  ARG A N   1 
ATOM   258  C  CA  . ARG A 1 88  ? 46.314  4.353   13.697  1.00 27.36 ? 88  ARG A CA  1 
ATOM   259  C  C   . ARG A 1 88  ? 46.439  3.246   14.745  1.00 29.01 ? 88  ARG A C   1 
ATOM   260  O  O   . ARG A 1 88  ? 45.561  2.381   14.851  1.00 24.33 ? 88  ARG A O   1 
ATOM   261  C  CB  . ARG A 1 88  ? 47.213  4.042   12.508  1.00 28.03 ? 88  ARG A CB  1 
ATOM   262  C  CG  . ARG A 1 88  ? 46.729  2.825   11.733  1.00 32.13 ? 88  ARG A CG  1 
ATOM   263  C  CD  . ARG A 1 88  ? 47.689  1.692   11.454  1.00 41.06 ? 88  ARG A CD  1 
ATOM   264  N  NE  . ARG A 1 88  ? 48.042  1.666   10.058  1.00 41.34 ? 88  ARG A NE  1 
ATOM   265  C  CZ  . ARG A 1 88  ? 47.384  1.069   9.081   1.00 39.18 ? 88  ARG A CZ  1 
ATOM   266  N  NH1 . ARG A 1 88  ? 47.599  -0.214  8.793   1.00 33.13 ? 88  ARG A NH1 1 
ATOM   267  N  NH2 . ARG A 1 88  ? 46.733  1.854   8.232   1.00 46.10 ? 88  ARG A NH2 1 
ATOM   268  N  N   . ALA A 1 89  ? 47.531  3.294   15.543  1.00 26.02 ? 89  ALA A N   1 
ATOM   269  C  CA  . ALA A 1 89  ? 47.783  2.290   16.569  1.00 24.64 ? 89  ALA A CA  1 
ATOM   270  C  C   . ALA A 1 89  ? 46.647  2.287   17.601  1.00 24.08 ? 89  ALA A C   1 
ATOM   271  O  O   . ALA A 1 89  ? 46.258  1.228   18.055  1.00 25.80 ? 89  ALA A O   1 
ATOM   272  C  CB  . ALA A 1 89  ? 49.148  2.495   17.245  1.00 20.67 ? 89  ALA A CB  1 
ATOM   273  N  N   . ALA A 1 90  ? 46.203  3.470   18.043  1.00 24.64 ? 90  ALA A N   1 
ATOM   274  C  CA  . ALA A 1 90  ? 45.158  3.586   19.038  1.00 25.51 ? 90  ALA A CA  1 
ATOM   275  C  C   . ALA A 1 90  ? 43.848  3.001   18.473  1.00 29.58 ? 90  ALA A C   1 
ATOM   276  O  O   . ALA A 1 90  ? 43.067  2.366   19.190  1.00 28.25 ? 90  ALA A O   1 
ATOM   277  C  CB  . ALA A 1 90  ? 44.980  5.038   19.454  1.00 27.33 ? 90  ALA A CB  1 
ATOM   278  N  N   . PHE A 1 91  ? 43.624  3.183   17.162  1.00 25.61 ? 91  PHE A N   1 
ATOM   279  C  CA  . PHE A 1 91  ? 42.391  2.667   16.564  1.00 24.73 ? 91  PHE A CA  1 
ATOM   280  C  C   . PHE A 1 91  ? 42.446  1.137   16.477  1.00 24.02 ? 91  PHE A C   1 
ATOM   281  O  O   . PHE A 1 91  ? 41.459  0.449   16.787  1.00 21.36 ? 91  PHE A O   1 
ATOM   282  C  CB  . PHE A 1 91  ? 42.155  3.322   15.213  1.00 26.27 ? 91  PHE A CB  1 
ATOM   283  C  CG  . PHE A 1 91  ? 40.804  2.950   14.686  1.00 26.45 ? 91  PHE A CG  1 
ATOM   284  C  CD1 . PHE A 1 91  ? 39.678  3.443   15.324  1.00 28.78 ? 91  PHE A CD1 1 
ATOM   285  C  CD2 . PHE A 1 91  ? 40.687  2.121   13.591  1.00 25.76 ? 91  PHE A CD2 1 
ATOM   286  C  CE1 . PHE A 1 91  ? 38.423  3.094   14.858  1.00 29.41 ? 91  PHE A CE1 1 
ATOM   287  C  CE2 . PHE A 1 91  ? 39.429  1.731   13.153  1.00 28.17 ? 91  PHE A CE2 1 
ATOM   288  C  CZ  . PHE A 1 91  ? 38.309  2.233   13.789  1.00 27.46 ? 91  PHE A CZ  1 
ATOM   289  N  N   . VAL A 1 92  ? 43.593  0.604   16.056  1.00 24.76 ? 92  VAL A N   1 
ATOM   290  C  CA  . VAL A 1 92  ? 43.814  -0.826  16.017  1.00 24.19 ? 92  VAL A CA  1 
ATOM   291  C  C   . VAL A 1 92  ? 43.618  -1.452  17.410  1.00 22.21 ? 92  VAL A C   1 
ATOM   292  O  O   . VAL A 1 92  ? 42.992  -2.493  17.562  1.00 23.46 ? 92  VAL A O   1 
ATOM   293  C  CB  . VAL A 1 92  ? 45.155  -1.177  15.380  1.00 23.33 ? 92  VAL A CB  1 
ATOM   294  C  CG1 . VAL A 1 92  ? 45.435  -2.667  15.553  1.00 25.71 ? 92  VAL A CG1 1 
ATOM   295  C  CG2 . VAL A 1 92  ? 45.207  -0.817  13.917  1.00 24.36 ? 92  VAL A CG2 1 
ATOM   296  N  N   . ALA A 1 93  ? 44.113  -0.766  18.442  1.00 23.38 ? 93  ALA A N   1 
ATOM   297  C  CA  . ALA A 1 93  ? 43.980  -1.196  19.824  1.00 21.10 ? 93  ALA A CA  1 
ATOM   298  C  C   . ALA A 1 93  ? 42.517  -1.296  20.224  1.00 20.46 ? 93  ALA A C   1 
ATOM   299  O  O   . ALA A 1 93  ? 42.117  -2.259  20.899  1.00 19.86 ? 93  ALA A O   1 
ATOM   300  C  CB  . ALA A 1 93  ? 44.758  -0.280  20.745  1.00 23.35 ? 93  ALA A CB  1 
ATOM   301  N  N   . LEU A 1 94  ? 41.732  -0.310  19.818  1.00 19.56 ? 94  LEU A N   1 
ATOM   302  C  CA  . LEU A 1 94  ? 40.303  -0.300  20.038  1.00 19.62 ? 94  LEU A CA  1 
ATOM   303  C  C   . LEU A 1 94  ? 39.613  -1.478  19.338  1.00 18.82 ? 94  LEU A C   1 
ATOM   304  O  O   . LEU A 1 94  ? 38.748  -2.129  19.945  1.00 18.25 ? 94  LEU A O   1 
ATOM   305  C  CB  . LEU A 1 94  ? 39.680  0.995   19.488  1.00 22.77 ? 94  LEU A CB  1 
ATOM   306  C  CG  . LEU A 1 94  ? 38.152  1.055   19.573  1.00 23.81 ? 94  LEU A CG  1 
ATOM   307  C  CD1 . LEU A 1 94  ? 37.757  1.180   21.024  1.00 25.71 ? 94  LEU A CD1 1 
ATOM   308  C  CD2 . LEU A 1 94  ? 37.595  2.188   18.764  1.00 28.01 ? 94  LEU A CD2 1 
ATOM   309  N  N   . LEU A 1 95  ? 39.985  -1.761  18.083  1.00 20.83 ? 95  LEU A N   1 
ATOM   310  C  CA  . LEU A 1 95  ? 39.372  -2.863  17.350  1.00 20.13 ? 95  LEU A CA  1 
ATOM   311  C  C   . LEU A 1 95  ? 39.621  -4.165  18.113  1.00 20.26 ? 95  LEU A C   1 
ATOM   312  O  O   . LEU A 1 95  ? 38.754  -5.018  18.197  1.00 18.86 ? 95  LEU A O   1 
ATOM   313  C  CB  . LEU A 1 95  ? 39.897  -2.979  15.911  1.00 18.17 ? 95  LEU A CB  1 
ATOM   314  C  CG  . LEU A 1 95  ? 39.470  -1.850  14.994  1.00 23.11 ? 95  LEU A CG  1 
ATOM   315  C  CD1 . LEU A 1 95  ? 40.181  -1.964  13.683  1.00 22.64 ? 95  LEU A CD1 1 
ATOM   316  C  CD2 . LEU A 1 95  ? 37.942  -1.770  14.852  1.00 24.74 ? 95  LEU A CD2 1 
ATOM   317  N  N   . LYS A 1 96  ? 40.837  -4.349  18.620  1.00 18.94 ? 96  LYS A N   1 
ATOM   318  C  CA  . LYS A 1 96  ? 41.131  -5.578  19.356  1.00 19.83 ? 96  LYS A CA  1 
ATOM   319  C  C   . LYS A 1 96  ? 40.356  -5.648  20.664  1.00 19.27 ? 96  LYS A C   1 
ATOM   320  O  O   . LYS A 1 96  ? 39.862  -6.695  21.040  1.00 21.40 ? 96  LYS A O   1 
ATOM   321  C  CB  . LYS A 1 96  ? 42.628  -5.673  19.680  1.00 21.86 ? 96  LYS A CB  1 
ATOM   322  C  CG  . LYS A 1 96  ? 43.445  -5.769  18.429  1.00 22.90 ? 96  LYS A CG  1 
ATOM   323  C  CD  . LYS A 1 96  ? 44.894  -5.800  18.688  1.00 27.67 ? 96  LYS A CD  1 
ATOM   324  C  CE  . LYS A 1 96  ? 45.666  -6.034  17.410  1.00 29.37 ? 96  LYS A CE  1 
ATOM   325  N  NZ  . LYS A 1 96  ? 47.042  -6.436  17.762  1.00 35.93 ? 96  LYS A NZ  1 
ATOM   326  N  N   . GLU A 1 97  ? 40.238  -4.534  21.376  1.00 20.95 ? 97  GLU A N   1 
ATOM   327  C  CA  . GLU A 1 97  ? 39.504  -4.505  22.631  1.00 24.03 ? 97  GLU A CA  1 
ATOM   328  C  C   . GLU A 1 97  ? 38.029  -4.754  22.392  1.00 19.80 ? 97  GLU A C   1 
ATOM   329  O  O   . GLU A 1 97  ? 37.393  -5.415  23.187  1.00 17.52 ? 97  GLU A O   1 
ATOM   330  C  CB  . GLU A 1 97  ? 39.645  -3.152  23.334  1.00 25.88 ? 97  GLU A CB  1 
ATOM   331  C  CG  . GLU A 1 97  ? 40.900  -3.070  24.188  1.00 39.21 ? 97  GLU A CG  1 
ATOM   332  C  CD  . GLU A 1 97  ? 40.904  -1.865  25.102  1.00 44.64 ? 97  GLU A CD  1 
ATOM   333  O  OE1 . GLU A 1 97  ? 41.757  -0.985  24.853  1.00 60.28 ? 97  GLU A OE1 1 
ATOM   334  O  OE2 . GLU A 1 97  ? 40.030  -1.805  26.028  1.00 54.98 ? 97  GLU A OE2 1 
ATOM   335  N  N   . TRP A 1 98  ? 37.485  -4.135  21.333  1.00 18.06 ? 98  TRP A N   1 
ATOM   336  C  CA  . TRP A 1 98  ? 36.097  -4.382  20.963  1.00 16.47 ? 98  TRP A CA  1 
ATOM   337  C  C   . TRP A 1 98  ? 35.846  -5.848  20.618  1.00 17.40 ? 98  TRP A C   1 
ATOM   338  O  O   . TRP A 1 98  ? 34.785  -6.402  20.945  1.00 16.67 ? 98  TRP A O   1 
ATOM   339  C  CB  . TRP A 1 98  ? 35.710  -3.496  19.762  1.00 17.09 ? 98  TRP A CB  1 
ATOM   340  C  CG  . TRP A 1 98  ? 35.194  -2.155  20.118  1.00 18.61 ? 98  TRP A CG  1 
ATOM   341  C  CD1 . TRP A 1 98  ? 35.128  -1.576  21.350  1.00 19.94 ? 98  TRP A CD1 1 
ATOM   342  C  CD2 . TRP A 1 98  ? 34.488  -1.259  19.225  1.00 19.42 ? 98  TRP A CD2 1 
ATOM   343  N  NE1 . TRP A 1 98  ? 34.505  -0.359  21.276  1.00 21.51 ? 98  TRP A NE1 1 
ATOM   344  C  CE2 . TRP A 1 98  ? 34.109  -0.139  19.982  1.00 19.38 ? 98  TRP A CE2 1 
ATOM   345  C  CE3 . TRP A 1 98  ? 34.184  -1.283  17.856  1.00 20.79 ? 98  TRP A CE3 1 
ATOM   346  C  CZ2 . TRP A 1 98  ? 33.367  0.903   19.433  1.00 21.90 ? 98  TRP A CZ2 1 
ATOM   347  C  CZ3 . TRP A 1 98  ? 33.493  -0.233  17.301  1.00 24.39 ? 98  TRP A CZ3 1 
ATOM   348  C  CH2 . TRP A 1 98  ? 33.108  0.849   18.086  1.00 20.25 ? 98  TRP A CH2 1 
ATOM   349  N  N   . THR A 1 99  ? 36.772  -6.448  19.860  1.00 17.53 ? 99  THR A N   1 
ATOM   350  C  CA  . THR A 1 99  ? 36.629  -7.845  19.508  1.00 17.79 ? 99  THR A CA  1 
ATOM   351  C  C   . THR A 1 99  ? 36.641  -8.741  20.768  1.00 17.64 ? 99  THR A C   1 
ATOM   352  O  O   . THR A 1 99  ? 35.809  -9.651  20.878  1.00 15.31 ? 99  THR A O   1 
ATOM   353  C  CB  . THR A 1 99  ? 37.752  -8.338  18.587  1.00 18.31 ? 99  THR A CB  1 
ATOM   354  O  OG1 . THR A 1 99  ? 37.844  -7.518  17.439  1.00 16.95 ? 99  THR A OG1 1 
ATOM   355  C  CG2 . THR A 1 99  ? 37.471  -9.763  18.171  1.00 20.58 ? 99  THR A CG2 1 
ATOM   356  N  N   . ALA A 1 100 ? 37.523  -8.471  21.735  1.00 16.16 ? 100 ALA A N   1 
ATOM   357  C  CA  . ALA A 1 100 ? 37.516  -9.179  23.018  1.00 16.29 ? 100 ALA A CA  1 
ATOM   358  C  C   . ALA A 1 100 ? 36.192  -9.033  23.752  1.00 15.14 ? 100 ALA A C   1 
ATOM   359  O  O   . ALA A 1 100 ? 35.618  -10.004 24.239  1.00 16.44 ? 100 ALA A O   1 
ATOM   360  C  CB  . ALA A 1 100 ? 38.636  -8.694  23.935  1.00 16.96 ? 100 ALA A CB  1 
ATOM   361  N  N   . ALA A 1 101 ? 35.685  -7.784  23.794  1.00 16.39 ? 101 ALA A N   1 
ATOM   362  C  CA  . ALA A 1 101 ? 34.386  -7.502  24.381  1.00 15.92 ? 101 ALA A CA  1 
ATOM   363  C  C   . ALA A 1 101 ? 33.247  -8.264  23.677  1.00 14.86 ? 101 ALA A C   1 
ATOM   364  O  O   . ALA A 1 101 ? 32.410  -8.903  24.336  1.00 15.09 ? 101 ALA A O   1 
ATOM   365  C  CB  . ALA A 1 101 ? 34.187  -6.026  24.409  1.00 16.56 ? 101 ALA A CB  1 
ATOM   366  N  N   . ALA A 1 102 ? 33.265  -8.320  22.344  1.00 15.09 ? 102 ALA A N   1 
ATOM   367  C  CA  . ALA A 1 102 ? 32.242  -8.993  21.567  1.00 14.86 ? 102 ALA A CA  1 
ATOM   368  C  C   . ALA A 1 102 ? 32.209  -10.471 21.894  1.00 15.00 ? 102 ALA A C   1 
ATOM   369  O  O   . ALA A 1 102 ? 31.160  -11.062 21.983  1.00 14.67 ? 102 ALA A O   1 
ATOM   370  C  CB  . ALA A 1 102 ? 32.468  -8.745  20.084  1.00 15.76 ? 102 ALA A CB  1 
ATOM   371  N  N   . ARG A 1 103 ? 33.372  -11.125 21.985  1.00 14.18 ? 103 ARG A N   1 
ATOM   372  C  CA  . ARG A 1 103 ? 33.371  -12.535 22.323  1.00 17.05 ? 103 ARG A CA  1 
ATOM   373  C  C   . ARG A 1 103 ? 32.749  -12.812 23.679  1.00 18.63 ? 103 ARG A C   1 
ATOM   374  O  O   . ARG A 1 103 ? 32.107  -13.831 23.811  1.00 16.37 ? 103 ARG A O   1 
ATOM   375  C  CB  . ARG A 1 103 ? 34.784  -13.126 22.453  1.00 19.24 ? 103 ARG A CB  1 
ATOM   376  C  CG  . ARG A 1 103 ? 35.547  -13.127 21.157  1.00 17.98 ? 103 ARG A CG  1 
ATOM   377  C  CD  . ARG A 1 103 ? 36.889  -13.852 21.407  1.00 18.54 ? 103 ARG A CD  1 
ATOM   378  N  NE  . ARG A 1 103 ? 37.578  -13.855 20.148  1.00 17.51 ? 103 ARG A NE  1 
ATOM   379  C  CZ  . ARG A 1 103 ? 38.471  -12.982 19.739  1.00 15.42 ? 103 ARG A CZ  1 
ATOM   380  N  NH1 . ARG A 1 103 ? 39.006  -12.086 20.557  1.00 16.24 ? 103 ARG A NH1 1 
ATOM   381  N  NH2 . ARG A 1 103 ? 38.901  -13.075 18.495  1.00 17.32 ? 103 ARG A NH2 1 
ATOM   382  N  N   . ARG A 1 104 ? 32.895  -11.920 24.667  1.00 16.95 ? 104 ARG A N   1 
ATOM   383  C  CA  . ARG A 1 104 ? 32.224  -12.042 25.949  1.00 18.07 ? 104 ARG A CA  1 
ATOM   384  C  C   . ARG A 1 104 ? 30.724  -11.802 25.781  1.00 15.60 ? 104 ARG A C   1 
ATOM   385  O  O   . ARG A 1 104 ? 29.881  -12.579 26.192  1.00 14.99 ? 104 ARG A O   1 
ATOM   386  C  CB  . ARG A 1 104 ? 32.804  -11.078 27.022  1.00 16.53 ? 104 ARG A CB  1 
ATOM   387  C  CG  . ARG A 1 104 ? 34.264  -11.248 27.426  1.00 22.23 ? 104 ARG A CG  1 
ATOM   388  C  CD  . ARG A 1 104 ? 34.506  -12.565 28.091  1.00 22.37 ? 104 ARG A CD  1 
ATOM   389  N  NE  . ARG A 1 104 ? 33.987  -12.495 29.422  1.00 25.49 ? 104 ARG A NE  1 
ATOM   390  C  CZ  . ARG A 1 104 ? 34.193  -13.487 30.291  1.00 25.86 ? 104 ARG A CZ  1 
ATOM   391  N  NH1 . ARG A 1 104 ? 34.588  -14.665 29.830  1.00 23.16 ? 104 ARG A NH1 1 
ATOM   392  N  NH2 . ARG A 1 104 ? 33.993  -13.235 31.562  1.00 31.03 ? 104 ARG A NH2 1 
ATOM   393  N  N   . LEU A 1 105 ? 30.352  -10.681 25.136  1.00 14.08 ? 105 LEU A N   1 
ATOM   394  C  CA  . LEU A 1 105 ? 28.970  -10.287 25.041  1.00 14.33 ? 105 LEU A CA  1 
ATOM   395  C  C   . LEU A 1 105 ? 28.129  -11.338 24.326  1.00 16.43 ? 105 LEU A C   1 
ATOM   396  O  O   . LEU A 1 105 ? 27.014  -11.637 24.782  1.00 16.22 ? 105 LEU A O   1 
ATOM   397  C  CB  . LEU A 1 105 ? 28.874  -8.954  24.312  1.00 14.91 ? 105 LEU A CB  1 
ATOM   398  C  CG  . LEU A 1 105 ? 29.467  -7.749  25.045  1.00 14.97 ? 105 LEU A CG  1 
ATOM   399  C  CD1 . LEU A 1 105 ? 29.696  -6.583  24.046  1.00 16.41 ? 105 LEU A CD1 1 
ATOM   400  C  CD2 . LEU A 1 105 ? 28.599  -7.280  26.218  1.00 18.01 ? 105 LEU A CD2 1 
ATOM   401  N  N   . THR A 1 106 ? 28.647  -11.859 23.187  1.00 14.16 ? 106 THR A N   1 
ATOM   402  C  CA  . THR A 1 106 ? 27.868  -12.815 22.442  1.00 14.38 ? 106 THR A CA  1 
ATOM   403  C  C   . THR A 1 106 ? 27.760  -14.184 23.135  1.00 16.75 ? 106 THR A C   1 
ATOM   404  O  O   . THR A 1 106 ? 26.876  -14.938 22.766  1.00 16.33 ? 106 THR A O   1 
ATOM   405  C  CB  . THR A 1 106 ? 28.393  -13.034 21.019  1.00 14.67 ? 106 THR A CB  1 
ATOM   406  O  OG1 . THR A 1 106 ? 29.771  -13.391 21.092  1.00 18.37 ? 106 THR A OG1 1 
ATOM   407  C  CG2 . THR A 1 106 ? 28.279  -11.772 20.224  1.00 15.09 ? 106 THR A CG2 1 
ATOM   408  N  N   . ALA A 1 107 ? 28.529  -14.434 24.219  1.00 15.62 ? 107 ALA A N   1 
ATOM   409  C  CA  . ALA A 1 107 ? 28.405  -15.673 24.972  1.00 18.06 ? 107 ALA A CA  1 
ATOM   410  C  C   . ALA A 1 107 ? 27.612  -15.445 26.261  1.00 21.05 ? 107 ALA A C   1 
ATOM   411  O  O   . ALA A 1 107 ? 27.403  -16.377 27.027  1.00 23.38 ? 107 ALA A O   1 
ATOM   412  C  CB  . ALA A 1 107 ? 29.791  -16.200 25.290  1.00 19.53 ? 107 ALA A CB  1 
ATOM   413  N  N   . GLY A 1 108 ? 27.172  -14.194 26.501  1.00 17.50 ? 108 GLY A N   1 
ATOM   414  C  CA  . GLY A 1 108 ? 26.388  -13.893 27.668  1.00 19.45 ? 108 GLY A CA  1 
ATOM   415  C  C   . GLY A 1 108 ? 27.278  -13.621 28.863  1.00 19.43 ? 108 GLY A C   1 
ATOM   416  O  O   . GLY A 1 108 ? 26.818  -13.646 29.994  1.00 21.03 ? 108 GLY A O   1 
ATOM   417  N  N   . HIS A 1 109 ? 28.557  -13.324 28.631  1.00 17.46 ? 109 HIS A N   1 
ATOM   418  C  CA  . HIS A 1 109 ? 29.424  -12.944 29.743  1.00 17.91 ? 109 HIS A CA  1 
ATOM   419  C  C   . HIS A 1 109 ? 29.633  -11.433 29.760  1.00 17.49 ? 109 HIS A C   1 
ATOM   420  O  O   . HIS A 1 109 ? 29.627  -10.750 28.765  1.00 17.24 ? 109 HIS A O   1 
ATOM   421  C  CB  . HIS A 1 109 ? 30.801  -13.616 29.664  1.00 22.18 ? 109 HIS A CB  1 
ATOM   422  C  CG  . HIS A 1 109 ? 30.754  -15.093 29.434  1.00 27.11 ? 109 HIS A CG  1 
ATOM   423  N  ND1 . HIS A 1 109 ? 30.030  -15.941 30.220  1.00 33.06 ? 109 HIS A ND1 1 
ATOM   424  C  CD2 . HIS A 1 109 ? 31.278  -15.840 28.414  1.00 24.55 ? 109 HIS A CD2 1 
ATOM   425  C  CE1 . HIS A 1 109 ? 30.131  -17.188 29.733  1.00 27.28 ? 109 HIS A CE1 1 
ATOM   426  N  NE2 . HIS A 1 109 ? 30.921  -17.143 28.621  1.00 27.25 ? 109 HIS A NE2 1 
ATOM   427  N  N   . ALA A 1 110 ? 30.011  -10.930 30.928  1.00 18.75 ? 110 ALA A N   1 
ATOM   428  C  CA  . ALA A 1 110 ? 30.260  -9.524  31.146  1.00 18.81 ? 110 ALA A CA  1 
ATOM   429  C  C   . ALA A 1 110 ? 31.625  -9.205  30.595  1.00 19.39 ? 110 ALA A C   1 
ATOM   430  O  O   . ALA A 1 110 ? 32.497  -10.083 30.503  1.00 20.69 ? 110 ALA A O   1 
ATOM   431  C  CB  . ALA A 1 110 ? 30.237  -9.257  32.686  1.00 19.76 ? 110 ALA A CB  1 
ATOM   432  N  N   . VAL A 1 111 ? 31.775  -7.975  30.129  1.00 19.09 ? 111 VAL A N   1 
ATOM   433  C  CA  . VAL A 1 111 ? 33.043  -7.495  29.598  1.00 23.15 ? 111 VAL A CA  1 
ATOM   434  C  C   . VAL A 1 111 ? 34.083  -7.344  30.708  1.00 22.34 ? 111 VAL A C   1 
ATOM   435  O  O   . VAL A 1 111 ? 33.751  -7.089  31.880  1.00 20.55 ? 111 VAL A O   1 
ATOM   436  C  CB  . VAL A 1 111 ? 32.890  -6.205  28.745  1.00 24.93 ? 111 VAL A CB  1 
ATOM   437  C  CG1 . VAL A 1 111 ? 31.842  -6.423  27.663  1.00 23.62 ? 111 VAL A CG1 1 
ATOM   438  C  CG2 . VAL A 1 111 ? 32.559  -4.987  29.521  1.00 30.05 ? 111 VAL A CG2 1 
ATOM   439  N  N   . GLY A 1 112 ? 35.357  -7.410  30.280  1.00 21.63 ? 112 GLY A N   1 
ATOM   440  C  CA  . GLY A 1 112 ? 36.485  -7.168  31.145  1.00 24.26 ? 112 GLY A CA  1 
ATOM   441  C  C   . GLY A 1 112 ? 36.420  -8.063  32.389  1.00 25.54 ? 112 GLY A C   1 
ATOM   442  O  O   . GLY A 1 112 ? 36.210  -9.283  32.331  1.00 24.35 ? 112 GLY A O   1 
ATOM   443  N  N   . GLU A 1 113 ? 36.646  -7.443  33.551  1.00 23.67 ? 113 GLU A N   1 
ATOM   444  C  CA  . GLU A 1 113 ? 36.660  -8.192  34.800  1.00 27.94 ? 113 GLU A CA  1 
ATOM   445  C  C   . GLU A 1 113 ? 35.279  -8.330  35.425  1.00 24.65 ? 113 GLU A C   1 
ATOM   446  O  O   . GLU A 1 113 ? 35.179  -8.743  36.563  1.00 27.83 ? 113 GLU A O   1 
ATOM   447  C  CB  . GLU A 1 113 ? 37.627  -7.497  35.750  1.00 35.74 ? 113 GLU A CB  1 
ATOM   448  C  CG  . GLU A 1 113 ? 38.969  -7.322  35.078  1.00 43.14 ? 113 GLU A CG  1 
ATOM   449  C  CD  . GLU A 1 113 ? 40.133  -7.570  36.006  1.00 54.20 ? 113 GLU A CD  1 
ATOM   450  O  OE1 . GLU A 1 113 ? 40.096  -8.589  36.765  1.00 55.89 ? 113 GLU A OE1 1 
ATOM   451  O  OE2 . GLU A 1 113 ? 41.063  -6.747  35.949  1.00 50.19 ? 113 GLU A OE2 1 
ATOM   452  N  N   . GLY A 1 114 ? 34.239  -7.844  34.744  1.00 20.75 ? 114 GLY A N   1 
ATOM   453  C  CA  . GLY A 1 114 ? 32.876  -8.100  35.098  1.00 18.65 ? 114 GLY A CA  1 
ATOM   454  C  C   . GLY A 1 114 ? 32.190  -6.836  35.617  1.00 21.13 ? 114 GLY A C   1 
ATOM   455  O  O   . GLY A 1 114 ? 32.715  -5.699  35.544  1.00 19.97 ? 114 GLY A O   1 
ATOM   456  N  N   . ALA A 1 115 ? 31.019  -7.100  36.185  1.00 19.52 ? 115 ALA A N   1 
ATOM   457  C  CA  . ALA A 1 115 ? 30.060  -6.074  36.508  1.00 20.89 ? 115 ALA A CA  1 
ATOM   458  C  C   . ALA A 1 115 ? 30.062  -5.700  37.988  1.00 23.89 ? 115 ALA A C   1 
ATOM   459  O  O   . ALA A 1 115 ? 29.451  -4.709  38.372  1.00 26.85 ? 115 ALA A O   1 
ATOM   460  C  CB  . ALA A 1 115 ? 28.731  -6.595  36.086  1.00 21.23 ? 115 ALA A CB  1 
ATOM   461  N  N   . TYR A 1 116 ? 30.790  -6.467  38.804  1.00 25.32 ? 116 TYR A N   1 
ATOM   462  C  CA  . TYR A 1 116 ? 30.883  -6.157  40.235  1.00 28.10 ? 116 TYR A CA  1 
ATOM   463  C  C   . TYR A 1 116 ? 31.986  -7.023  40.826  1.00 25.39 ? 116 TYR A C   1 
ATOM   464  O  O   . TYR A 1 116 ? 32.528  -7.815  40.101  1.00 26.72 ? 116 TYR A O   1 
ATOM   465  C  CB  . TYR A 1 116 ? 29.570  -6.389  40.980  1.00 29.15 ? 116 TYR A CB  1 
ATOM   466  C  CG  . TYR A 1 116 ? 29.091  -7.817  40.945  1.00 33.47 ? 116 TYR A CG  1 
ATOM   467  C  CD1 . TYR A 1 116 ? 28.374  -8.297  39.869  1.00 30.18 ? 116 TYR A CD1 1 
ATOM   468  C  CD2 . TYR A 1 116 ? 29.359  -8.693  41.989  1.00 34.40 ? 116 TYR A CD2 1 
ATOM   469  C  CE1 . TYR A 1 116 ? 27.946  -9.614  39.808  1.00 32.14 ? 116 TYR A CE1 1 
ATOM   470  C  CE2 . TYR A 1 116 ? 28.897  -9.999  41.970  1.00 34.89 ? 116 TYR A CE2 1 
ATOM   471  C  CZ  . TYR A 1 116 ? 28.212  -10.471 40.862  1.00 35.67 ? 116 TYR A CZ  1 
ATOM   472  O  OH  . TYR A 1 116 ? 27.754  -11.772 40.807  1.00 37.76 ? 116 TYR A OH  1 
ATOM   473  N  N   . GLY A 1 117 ? 32.361  -6.796  42.085  1.00 32.40 ? 117 GLY A N   1 
ATOM   474  C  CA  . GLY A 1 117 ? 33.340  -7.643  42.746  1.00 36.30 ? 117 GLY A CA  1 
ATOM   475  C  C   . GLY A 1 117 ? 34.768  -7.199  42.458  1.00 38.03 ? 117 GLY A C   1 
ATOM   476  O  O   . GLY A 1 117 ? 35.724  -7.839  42.895  1.00 49.16 ? 117 GLY A O   1 
ATOM   477  N  N   . GLY A 1 118 ? 34.917  -6.089  41.723  1.00 35.98 ? 118 GLY A N   1 
ATOM   478  C  CA  . GLY A 1 118 ? 36.196  -5.409  41.595  1.00 33.78 ? 118 GLY A CA  1 
ATOM   479  C  C   . GLY A 1 118 ? 36.475  -4.494  42.782  1.00 30.24 ? 118 GLY A C   1 
ATOM   480  O  O   . GLY A 1 118 ? 35.732  -4.494  43.781  1.00 30.42 ? 118 GLY A O   1 
ATOM   481  N  N   . LEU A 1 119 ? 37.486  -3.650  42.586  1.00 31.31 ? 119 LEU A N   1 
ATOM   482  C  CA  . LEU A 1 119 ? 37.897  -2.652  43.551  1.00 40.22 ? 119 LEU A CA  1 
ATOM   483  C  C   . LEU A 1 119 ? 36.698  -1.713  43.738  1.00 36.37 ? 119 LEU A C   1 
ATOM   484  O  O   . LEU A 1 119 ? 36.140  -1.241  42.739  1.00 31.90 ? 119 LEU A O   1 
ATOM   485  C  CB  . LEU A 1 119 ? 39.135  -1.899  43.030  1.00 45.41 ? 119 LEU A CB  1 
ATOM   486  C  CG  . LEU A 1 119 ? 40.452  -2.682  42.883  1.00 50.48 ? 119 LEU A CG  1 
ATOM   487  C  CD1 . LEU A 1 119 ? 41.551  -1.752  42.376  1.00 52.37 ? 119 LEU A CD1 1 
ATOM   488  C  CD2 . LEU A 1 119 ? 40.893  -3.381  44.182  1.00 48.71 ? 119 LEU A CD2 1 
ATOM   489  N  N   . PRO A 1 120 ? 36.251  -1.476  44.990  1.00 31.84 ? 120 PRO A N   1 
ATOM   490  C  CA  . PRO A 1 120 ? 35.177  -0.527  45.281  1.00 34.14 ? 120 PRO A CA  1 
ATOM   491  C  C   . PRO A 1 120 ? 35.363  0.852   44.667  1.00 33.40 ? 120 PRO A C   1 
ATOM   492  O  O   . PRO A 1 120 ? 34.388  1.518   44.337  1.00 22.81 ? 120 PRO A O   1 
ATOM   493  C  CB  . PRO A 1 120 ? 35.187  -0.385  46.826  1.00 35.43 ? 120 PRO A CB  1 
ATOM   494  C  CG  . PRO A 1 120 ? 35.853  -1.625  47.351  1.00 32.66 ? 120 PRO A CG  1 
ATOM   495  C  CD  . PRO A 1 120 ? 36.649  -2.218  46.208  1.00 33.52 ? 120 PRO A CD  1 
ATOM   496  N  N   . GLU A 1 121 ? 36.616  1.326   44.548  1.00 26.92 ? 121 GLU A N   1 
ATOM   497  C  CA  . GLU A 1 121 ? 36.814  2.693   44.129  1.00 26.49 ? 121 GLU A CA  1 
ATOM   498  C  C   . GLU A 1 121 ? 36.961  2.814   42.609  1.00 25.34 ? 121 GLU A C   1 
ATOM   499  O  O   . GLU A 1 121 ? 37.250  3.900   42.127  1.00 31.44 ? 121 GLU A O   1 
ATOM   500  C  CB  . GLU A 1 121 ? 37.991  3.317   44.913  1.00 35.11 ? 121 GLU A CB  1 
ATOM   501  C  CG  . GLU A 1 121 ? 39.326  2.629   44.713  1.00 41.51 ? 121 GLU A CG  1 
ATOM   502  C  CD  . GLU A 1 121 ? 39.581  1.313   45.438  1.00 45.32 ? 121 GLU A CD  1 
ATOM   503  O  OE1 . GLU A 1 121 ? 38.740  0.882   46.266  1.00 44.95 ? 121 GLU A OE1 1 
ATOM   504  O  OE2 . GLU A 1 121 ? 40.666  0.742   45.194  1.00 68.50 ? 121 GLU A OE2 1 
ATOM   505  N  N   . ALA A 1 122 ? 36.802  1.726   41.851  1.00 24.53 ? 122 ALA A N   1 
ATOM   506  C  CA  . ALA A 1 122 ? 36.848  1.826   40.395  1.00 24.44 ? 122 ALA A CA  1 
ATOM   507  C  C   . ALA A 1 122 ? 35.457  1.590   39.820  1.00 22.56 ? 122 ALA A C   1 
ATOM   508  O  O   . ALA A 1 122 ? 34.640  0.828   40.393  1.00 21.35 ? 122 ALA A O   1 
ATOM   509  C  CB  . ALA A 1 122 ? 37.801  0.796   39.833  1.00 27.77 ? 122 ALA A CB  1 
ATOM   510  N  N   . PRO A 1 123 ? 35.165  2.262   38.680  1.00 23.67 ? 123 PRO A N   1 
ATOM   511  C  CA  . PRO A 1 123 ? 33.964  1.964   37.899  1.00 20.50 ? 123 PRO A CA  1 
ATOM   512  C  C   . PRO A 1 123 ? 34.008  0.506   37.492  1.00 22.74 ? 123 PRO A C   1 
ATOM   513  O  O   . PRO A 1 123 ? 35.025  -0.015  37.072  1.00 22.51 ? 123 PRO A O   1 
ATOM   514  C  CB  . PRO A 1 123 ? 34.045  2.849   36.638  1.00 24.57 ? 123 PRO A CB  1 
ATOM   515  C  CG  . PRO A 1 123 ? 35.243  3.758   36.819  1.00 25.55 ? 123 PRO A CG  1 
ATOM   516  C  CD  . PRO A 1 123 ? 35.997  3.276   38.051  1.00 24.83 ? 123 PRO A CD  1 
ATOM   517  N  N   . PRO A 1 124 ? 32.891  -0.216  37.524  1.00 22.09 ? 124 PRO A N   1 
ATOM   518  C  CA  . PRO A 1 124 ? 32.896  -1.564  36.988  1.00 22.27 ? 124 PRO A CA  1 
ATOM   519  C  C   . PRO A 1 124 ? 33.207  -1.601  35.491  1.00 22.11 ? 124 PRO A C   1 
ATOM   520  O  O   . PRO A 1 124 ? 32.880  -0.685  34.733  1.00 20.80 ? 124 PRO A O   1 
ATOM   521  C  CB  . PRO A 1 124 ? 31.480  -2.036  37.198  1.00 21.65 ? 124 PRO A CB  1 
ATOM   522  C  CG  . PRO A 1 124 ? 30.649  -0.845  37.624  1.00 23.71 ? 124 PRO A CG  1 
ATOM   523  C  CD  . PRO A 1 124 ? 31.574  0.295   37.969  1.00 22.49 ? 124 PRO A CD  1 
ATOM   524  N  N   . ASP A 1 125 ? 33.839  -2.698  35.086  1.00 20.80 ? 125 ASP A N   1 
ATOM   525  C  CA  . ASP A 1 125 ? 34.258  -2.846  33.698  1.00 19.94 ? 125 ASP A CA  1 
ATOM   526  C  C   . ASP A 1 125 ? 33.045  -3.061  32.784  1.00 18.54 ? 125 ASP A C   1 
ATOM   527  O  O   . ASP A 1 125 ? 33.085  -2.681  31.612  1.00 21.99 ? 125 ASP A O   1 
ATOM   528  C  CB  . ASP A 1 125 ? 35.165  -4.069  33.478  1.00 22.73 ? 125 ASP A CB  1 
ATOM   529  C  CG  . ASP A 1 125 ? 36.642  -3.813  33.669  1.00 26.51 ? 125 ASP A CG  1 
ATOM   530  O  OD1 . ASP A 1 125 ? 36.998  -2.641  33.867  1.00 26.26 ? 125 ASP A OD1 1 
ATOM   531  O  OD2 . ASP A 1 125 ? 37.355  -4.777  33.618  1.00 29.22 ? 125 ASP A OD2 1 
ATOM   532  N  N   . ASP A 1 126 ? 32.010  -3.728  33.317  1.00 18.88 ? 126 ASP A N   1 
ATOM   533  C  CA  . ASP A 1 126 ? 30.766  -3.953  32.624  1.00 17.28 ? 126 ASP A CA  1 
ATOM   534  C  C   . ASP A 1 126 ? 29.684  -3.177  33.339  1.00 17.28 ? 126 ASP A C   1 
ATOM   535  O  O   . ASP A 1 126 ? 29.671  -3.219  34.575  1.00 16.76 ? 126 ASP A O   1 
ATOM   536  C  CB  . ASP A 1 126 ? 30.439  -5.441  32.583  1.00 18.67 ? 126 ASP A CB  1 
ATOM   537  C  CG  . ASP A 1 126 ? 29.262  -5.749  31.674  1.00 20.54 ? 126 ASP A CG  1 
ATOM   538  O  OD1 . ASP A 1 126 ? 28.154  -5.419  32.039  1.00 18.75 ? 126 ASP A OD1 1 
ATOM   539  O  OD2 . ASP A 1 126 ? 29.468  -6.379  30.647  1.00 20.13 ? 126 ASP A OD2 1 
ATOM   540  N  N   . THR A 1 127 ? 28.766  -2.531  32.588  1.00 16.57 ? 127 THR A N   1 
ATOM   541  C  CA  . THR A 1 127 ? 27.742  -1.670  33.194  1.00 17.84 ? 127 THR A CA  1 
ATOM   542  C  C   . THR A 1 127 ? 26.630  -2.409  33.912  1.00 18.05 ? 127 THR A C   1 
ATOM   543  O  O   . THR A 1 127 ? 25.848  -1.800  34.669  1.00 17.85 ? 127 THR A O   1 
ATOM   544  C  CB  . THR A 1 127 ? 27.166  -0.729  32.115  1.00 19.38 ? 127 THR A CB  1 
ATOM   545  O  OG1 . THR A 1 127 ? 26.560  -1.437  31.034  1.00 16.54 ? 127 THR A OG1 1 
ATOM   546  C  CG2 . THR A 1 127 ? 28.233  0.176   31.590  1.00 18.37 ? 127 THR A CG2 1 
ATOM   547  N  N   . GLY A 1 128 ? 26.512  -3.726  33.709  1.00 16.35 ? 128 GLY A N   1 
ATOM   548  C  CA  . GLY A 1 128 ? 25.783  -4.586  34.642  1.00 16.58 ? 128 GLY A CA  1 
ATOM   549  C  C   . GLY A 1 128 ? 24.332  -4.903  34.286  1.00 13.90 ? 128 GLY A C   1 
ATOM   550  O  O   . GLY A 1 128 ? 23.753  -5.726  34.959  1.00 19.58 ? 128 GLY A O   1 
ATOM   551  N  N   . GLU A 1 129 ? 23.687  -4.251  33.299  1.00 18.07 ? 129 GLU A N   1 
ATOM   552  C  CA  . GLU A 1 129 ? 22.240  -4.339  33.101  1.00 15.12 ? 129 GLU A CA  1 
ATOM   553  C  C   . GLU A 1 129 ? 21.849  -5.630  32.335  1.00 17.07 ? 129 GLU A C   1 
ATOM   554  O  O   . GLU A 1 129 ? 20.679  -5.889  32.226  1.00 19.35 ? 129 GLU A O   1 
ATOM   555  C  CB  . GLU A 1 129 ? 21.686  -3.093  32.403  1.00 17.18 ? 129 GLU A CB  1 
ATOM   556  C  CG  . GLU A 1 129 ? 21.963  -2.954  30.914  1.00 16.75 ? 129 GLU A CG  1 
ATOM   557  C  CD  . GLU A 1 129 ? 23.270  -2.247  30.578  1.00 15.97 ? 129 GLU A CD  1 
ATOM   558  O  OE1 . GLU A 1 129 ? 24.158  -2.173  31.426  1.00 16.29 ? 129 GLU A OE1 1 
ATOM   559  O  OE2 . GLU A 1 129 ? 23.350  -1.696  29.477  1.00 15.28 ? 129 GLU A OE2 1 
ATOM   560  N  N   . ALA A 1 130 ? 22.824  -6.423  31.876  1.00 16.04 ? 130 ALA A N   1 
ATOM   561  C  CA  . ALA A 1 130 ? 22.611  -7.718  31.258  1.00 16.27 ? 130 ALA A CA  1 
ATOM   562  C  C   . ALA A 1 130 ? 22.981  -8.861  32.224  1.00 18.70 ? 130 ALA A C   1 
ATOM   563  O  O   . ALA A 1 130 ? 22.851  -10.027 31.847  1.00 20.60 ? 130 ALA A O   1 
ATOM   564  C  CB  . ALA A 1 130 ? 23.447  -7.832  29.964  1.00 14.26 ? 130 ALA A CB  1 
ATOM   565  N  N   . LEU A 1 131 ? 23.378  -8.559  33.470  1.00 16.16 ? 131 LEU A N   1 
ATOM   566  C  CA  . LEU A 1 131 ? 23.585  -9.639  34.430  1.00 19.29 ? 131 LEU A CA  1 
ATOM   567  C  C   . LEU A 1 131 ? 22.346  -10.506 34.544  1.00 19.39 ? 131 LEU A C   1 
ATOM   568  O  O   . LEU A 1 131 ? 21.230  -10.029 34.637  1.00 22.53 ? 131 LEU A O   1 
ATOM   569  C  CB  . LEU A 1 131 ? 23.893  -9.136  35.825  1.00 21.97 ? 131 LEU A CB  1 
ATOM   570  C  CG  . LEU A 1 131 ? 25.292  -8.626  35.975  1.00 22.83 ? 131 LEU A CG  1 
ATOM   571  C  CD1 . LEU A 1 131 ? 25.362  -7.850  37.297  1.00 22.27 ? 131 LEU A CD1 1 
ATOM   572  C  CD2 . LEU A 1 131 ? 26.327  -9.768  35.863  1.00 27.82 ? 131 LEU A CD2 1 
ATOM   573  N  N   . GLY A 1 132 ? 22.608  -11.816 34.539  1.00 23.95 ? 132 GLY A N   1 
ATOM   574  C  CA  . GLY A 1 132 ? 21.556  -12.798 34.678  1.00 22.64 ? 132 GLY A CA  1 
ATOM   575  C  C   . GLY A 1 132 ? 20.776  -13.110 33.398  1.00 22.45 ? 132 GLY A C   1 
ATOM   576  O  O   . GLY A 1 132 ? 19.756  -13.812 33.452  1.00 28.80 ? 132 GLY A O   1 
ATOM   577  N  N   . LEU A 1 133 ? 21.121  -12.476 32.264  1.00 17.58 ? 133 LEU A N   1 
ATOM   578  C  CA  . LEU A 1 133 ? 20.342  -12.740 31.053  1.00 19.00 ? 133 LEU A CA  1 
ATOM   579  C  C   . LEU A 1 133 ? 21.109  -13.758 30.214  1.00 17.85 ? 133 LEU A C   1 
ATOM   580  O  O   . LEU A 1 133 ? 22.335  -13.782 30.271  1.00 25.50 ? 133 LEU A O   1 
ATOM   581  C  CB  . LEU A 1 133 ? 20.091  -11.440 30.272  1.00 22.20 ? 133 LEU A CB  1 
ATOM   582  C  CG  . LEU A 1 133 ? 19.431  -10.338 31.115  1.00 20.54 ? 133 LEU A CG  1 
ATOM   583  C  CD1 . LEU A 1 133 ? 19.169  -9.103  30.298  1.00 20.35 ? 133 LEU A CD1 1 
ATOM   584  C  CD2 . LEU A 1 133 ? 18.133  -10.845 31.733  1.00 19.85 ? 133 LEU A CD2 1 
ATOM   585  N  N   . LYS A 1 134 ? 20.381  -14.447 29.316  1.00 19.86 ? 134 LYS A N   1 
ATOM   586  C  CA  . LYS A 1 134 ? 20.960  -15.367 28.354  1.00 19.03 ? 134 LYS A CA  1 
ATOM   587  C  C   . LYS A 1 134 ? 21.541  -14.573 27.172  1.00 18.87 ? 134 LYS A C   1 
ATOM   588  O  O   . LYS A 1 134 ? 21.274  -13.367 26.985  1.00 19.16 ? 134 LYS A O   1 
ATOM   589  C  CB  . LYS A 1 134 ? 19.937  -16.419 27.917  1.00 21.28 ? 134 LYS A CB  1 
ATOM   590  C  CG  . LYS A 1 134 ? 19.428  -17.336 29.032  1.00 27.84 ? 134 LYS A CG  1 
ATOM   591  C  CD  . LYS A 1 134 ? 20.412  -18.444 29.439  1.00 33.86 ? 134 LYS A CD  1 
ATOM   592  N  N   . PRO A 1 135 ? 22.426  -15.233 26.389  1.00 22.06 ? 135 PRO A N   1 
ATOM   593  C  CA  . PRO A 1 135 ? 22.999  -14.593 25.205  1.00 19.90 ? 135 PRO A CA  1 
ATOM   594  C  C   . PRO A 1 135 ? 21.927  -14.051 24.274  1.00 18.50 ? 135 PRO A C   1 
ATOM   595  O  O   . PRO A 1 135 ? 22.153  -13.056 23.573  1.00 18.23 ? 135 PRO A O   1 
ATOM   596  C  CB  . PRO A 1 135 ? 23.812  -15.742 24.566  1.00 20.48 ? 135 PRO A CB  1 
ATOM   597  C  CG  . PRO A 1 135 ? 24.175  -16.705 25.688  1.00 23.70 ? 135 PRO A CG  1 
ATOM   598  C  CD  . PRO A 1 135 ? 23.024  -16.573 26.663  1.00 19.94 ? 135 PRO A CD  1 
ATOM   599  N  N   . SER A 1 136 ? 20.758  -14.711 24.222  1.00 15.82 ? 136 SER A N   1 
ATOM   600  C  CA  . SER A 1 136 ? 19.611  -14.245 23.445  1.00 16.02 ? 136 SER A CA  1 
ATOM   601  C  C   . SER A 1 136 ? 19.894  -14.039 21.937  1.00 17.85 ? 136 SER A C   1 
ATOM   602  O  O   . SER A 1 136 ? 19.374  -13.091 21.295  1.00 16.06 ? 136 SER A O   1 
ATOM   603  C  CB  . SER A 1 136 ? 19.062  -12.981 24.030  1.00 19.31 ? 136 SER A CB  1 
ATOM   604  O  OG  . SER A 1 136 ? 18.796  -13.173 25.430  1.00 23.22 ? 136 SER A OG  1 
ATOM   605  N  N   . ARG A 1 137 ? 20.780  -14.895 21.406  1.00 15.29 ? 137 ARG A N   1 
ATOM   606  C  CA  . ARG A 1 137 ? 21.191  -14.908 20.004  1.00 15.56 ? 137 ARG A CA  1 
ATOM   607  C  C   . ARG A 1 137 ? 21.779  -13.579 19.614  1.00 15.16 ? 137 ARG A C   1 
ATOM   608  O  O   . ARG A 1 137 ? 21.683  -13.219 18.432  1.00 15.29 ? 137 ARG A O   1 
ATOM   609  C  CB  . ARG A 1 137 ? 20.017  -15.232 19.085  1.00 15.13 ? 137 ARG A CB  1 
ATOM   610  C  CG  . ARG A 1 137 ? 19.379  -16.590 19.367  1.00 17.81 ? 137 ARG A CG  1 
ATOM   611  C  CD  . ARG A 1 137 ? 18.591  -17.102 18.159  1.00 19.74 ? 137 ARG A CD  1 
ATOM   612  N  NE  . ARG A 1 137 ? 17.419  -16.242 18.018  1.00 20.03 ? 137 ARG A NE  1 
ATOM   613  C  CZ  . ARG A 1 137 ? 16.609  -16.209 16.963  1.00 20.95 ? 137 ARG A CZ  1 
ATOM   614  N  NH1 . ARG A 1 137 ? 15.631  -15.305 16.845  1.00 20.09 ? 137 ARG A NH1 1 
ATOM   615  N  NH2 . ARG A 1 137 ? 16.792  -17.101 16.006  1.00 24.91 ? 137 ARG A NH2 1 
ATOM   616  N  N   . LEU A 1 138 ? 22.460  -12.922 20.548  1.00 14.42 ? 138 LEU A N   1 
ATOM   617  C  CA  . LEU A 1 138 ? 23.155  -11.692 20.207  1.00 16.47 ? 138 LEU A CA  1 
ATOM   618  C  C   . LEU A 1 138 ? 24.179  -11.915 19.104  1.00 14.07 ? 138 LEU A C   1 
ATOM   619  O  O   . LEU A 1 138 ? 25.064  -12.781 19.231  1.00 15.32 ? 138 LEU A O   1 
ATOM   620  C  CB  . LEU A 1 138 ? 23.837  -11.065 21.424  1.00 13.62 ? 138 LEU A CB  1 
ATOM   621  C  CG  . LEU A 1 138 ? 24.656  -9.794  21.150  1.00 14.54 ? 138 LEU A CG  1 
ATOM   622  C  CD1 . LEU A 1 138 ? 23.746  -8.572  20.765  1.00 13.37 ? 138 LEU A CD1 1 
ATOM   623  C  CD2 . LEU A 1 138 ? 25.506  -9.474  22.401  1.00 13.94 ? 138 LEU A CD2 1 
ATOM   624  N  N   . THR A 1 139 ? 24.056  -11.102 18.028  1.00 12.39 ? 139 THR A N   1 
ATOM   625  C  CA  . THR A 1 139 ? 25.159  -10.945 17.086  1.00 12.52 ? 139 THR A CA  1 
ATOM   626  C  C   . THR A 1 139 ? 25.616  -9.490  17.043  1.00 13.12 ? 139 THR A C   1 
ATOM   627  O  O   . THR A 1 139 ? 24.821  -8.566  17.282  1.00 12.68 ? 139 THR A O   1 
ATOM   628  C  CB  . THR A 1 139 ? 24.757  -11.456 15.712  1.00 12.19 ? 139 THR A CB  1 
ATOM   629  O  OG1 . THR A 1 139 ? 23.644  -10.721 15.216  1.00 11.75 ? 139 THR A OG1 1 
ATOM   630  C  CG2 . THR A 1 139 ? 24.463  -12.940 15.714  1.00 12.58 ? 139 THR A CG2 1 
ATOM   631  N  N   . LEU A 1 140 ? 26.900  -9.285  16.799  1.00 13.51 ? 140 LEU A N   1 
ATOM   632  C  CA  . LEU A 1 140 ? 27.513  -7.983  16.671  1.00 13.44 ? 140 LEU A CA  1 
ATOM   633  C  C   . LEU A 1 140 ? 28.297  -7.968  15.374  1.00 14.72 ? 140 LEU A C   1 
ATOM   634  O  O   . LEU A 1 140 ? 29.168  -8.785  15.163  1.00 17.03 ? 140 LEU A O   1 
ATOM   635  C  CB  . LEU A 1 140 ? 28.453  -7.663  17.834  1.00 14.72 ? 140 LEU A CB  1 
ATOM   636  C  CG  . LEU A 1 140 ? 27.753  -7.569  19.188  1.00 15.96 ? 140 LEU A CG  1 
ATOM   637  C  CD1 . LEU A 1 140 ? 28.770  -7.644  20.346  1.00 17.38 ? 140 LEU A CD1 1 
ATOM   638  C  CD2 . LEU A 1 140 ? 26.911  -6.290  19.210  1.00 14.40 ? 140 LEU A CD2 1 
ATOM   639  N  N   . THR A 1 141 ? 27.861  -7.096  14.470  1.00 11.82 ? 141 THR A N   1 
ATOM   640  C  CA  . THR A 1 141 ? 28.392  -7.023  13.105  1.00 13.62 ? 141 THR A CA  1 
ATOM   641  C  C   . THR A 1 141 ? 28.954  -5.624  12.904  1.00 12.98 ? 141 THR A C   1 
ATOM   642  O  O   . THR A 1 141 ? 28.220  -4.633  13.091  1.00 14.30 ? 141 THR A O   1 
ATOM   643  C  CB  . THR A 1 141 ? 27.268  -7.295  12.066  1.00 14.35 ? 141 THR A CB  1 
ATOM   644  O  OG1 . THR A 1 141 ? 26.548  -8.474  12.424  1.00 15.08 ? 141 THR A OG1 1 
ATOM   645  C  CG2 . THR A 1 141 ? 27.823  -7.406  10.657  1.00 15.03 ? 141 THR A CG2 1 
ATOM   646  N  N   . ILE A 1 142 ? 30.229  -5.551  12.535  1.00 13.33 ? 142 ILE A N   1 
ATOM   647  C  CA  . ILE A 1 142 ? 30.902  -4.278  12.353  1.00 13.93 ? 142 ILE A CA  1 
ATOM   648  C  C   . ILE A 1 142 ? 30.992  -3.988  10.862  1.00 13.99 ? 142 ILE A C   1 
ATOM   649  O  O   . ILE A 1 142 ? 31.222  -4.872  10.046  1.00 14.51 ? 142 ILE A O   1 
ATOM   650  C  CB  . ILE A 1 142 ? 32.297  -4.251  13.031  1.00 14.12 ? 142 ILE A CB  1 
ATOM   651  C  CG1 . ILE A 1 142 ? 32.874  -2.840  13.109  1.00 16.04 ? 142 ILE A CG1 1 
ATOM   652  C  CG2 . ILE A 1 142 ? 33.292  -5.195  12.364  1.00 13.79 ? 142 ILE A CG2 1 
ATOM   653  C  CD1 . ILE A 1 142 ? 34.029  -2.741  14.066  1.00 17.68 ? 142 ILE A CD1 1 
ATOM   654  N  N   . GLY A 1 143 ? 30.874  -2.710  10.517  1.00 13.90 ? 143 GLY A N   1 
ATOM   655  C  CA  . GLY A 1 143 ? 31.135  -2.241  9.178   1.00 14.53 ? 143 GLY A CA  1 
ATOM   656  C  C   . GLY A 1 143 ? 31.893  -0.920  9.168   1.00 14.60 ? 143 GLY A C   1 
ATOM   657  O  O   . GLY A 1 143 ? 31.910  -0.197  10.153  1.00 17.04 ? 143 GLY A O   1 
ATOM   658  N  N   . PHE A 1 144 ? 32.589  -0.686  8.059   1.00 14.65 ? 144 PHE A N   1 
ATOM   659  C  CA  . PHE A 1 144 ? 33.410  0.523   7.861   1.00 15.91 ? 144 PHE A CA  1 
ATOM   660  C  C   . PHE A 1 144 ? 32.826  1.391   6.737   1.00 15.92 ? 144 PHE A C   1 
ATOM   661  O  O   . PHE A 1 144 ? 32.558  0.894   5.647   1.00 17.51 ? 144 PHE A O   1 
ATOM   662  C  CB  . PHE A 1 144 ? 34.799  0.124   7.426   1.00 18.38 ? 144 PHE A CB  1 
ATOM   663  C  CG  . PHE A 1 144 ? 35.525  -0.773  8.396   1.00 16.35 ? 144 PHE A CG  1 
ATOM   664  C  CD1 . PHE A 1 144 ? 35.385  -0.544  9.759   1.00 19.55 ? 144 PHE A CD1 1 
ATOM   665  C  CD2 . PHE A 1 144 ? 36.295  -1.838  7.970   1.00 23.10 ? 144 PHE A CD2 1 
ATOM   666  C  CE1 . PHE A 1 144 ? 36.026  -1.360  10.697  1.00 20.84 ? 144 PHE A CE1 1 
ATOM   667  C  CE2 . PHE A 1 144 ? 36.956  -2.623  8.912   1.00 22.29 ? 144 PHE A CE2 1 
ATOM   668  C  CZ  . PHE A 1 144 ? 36.800  -2.379  10.275  1.00 22.55 ? 144 PHE A CZ  1 
ATOM   669  N  N   . GLY A 1 145 ? 32.582  2.652   7.043   1.00 17.09 ? 145 GLY A N   1 
ATOM   670  C  CA  . GLY A 1 145 ? 32.000  3.599   6.097   1.00 19.03 ? 145 GLY A CA  1 
ATOM   671  C  C   . GLY A 1 145 ? 33.045  4.207   5.170   1.00 19.47 ? 145 GLY A C   1 
ATOM   672  O  O   . GLY A 1 145 ? 34.253  4.177   5.418   1.00 17.45 ? 145 GLY A O   1 
ATOM   673  N  N   . PRO A 1 146 ? 32.611  4.727   4.018   1.00 19.45 ? 146 PRO A N   1 
ATOM   674  C  CA  . PRO A 1 146 ? 33.572  5.319   3.073   1.00 20.88 ? 146 PRO A CA  1 
ATOM   675  C  C   . PRO A 1 146 ? 34.481  6.389   3.696   1.00 21.13 ? 146 PRO A C   1 
ATOM   676  O  O   . PRO A 1 146 ? 35.663  6.451   3.352   1.00 25.57 ? 146 PRO A O   1 
ATOM   677  C  CB  . PRO A 1 146 ? 32.709  5.964   1.953   1.00 21.09 ? 146 PRO A CB  1 
ATOM   678  C  CG  . PRO A 1 146 ? 31.262  5.563   2.266   1.00 21.41 ? 146 PRO A CG  1 
ATOM   679  C  CD  . PRO A 1 146 ? 31.207  4.729   3.546   1.00 19.51 ? 146 PRO A CD  1 
ATOM   680  N  N   . SER A 1 147 ? 33.906  7.195   4.588   1.00 19.40 ? 147 SER A N   1 
ATOM   681  C  CA  . SER A 1 147 ? 34.594  8.258   5.305   1.00 22.13 ? 147 SER A CA  1 
ATOM   682  C  C   . SER A 1 147 ? 35.765  7.729   6.156   1.00 24.36 ? 147 SER A C   1 
ATOM   683  O  O   . SER A 1 147 ? 36.737  8.448   6.353   1.00 24.78 ? 147 SER A O   1 
ATOM   684  C  CB  . SER A 1 147 ? 33.644  9.142   6.096   1.00 24.33 ? 147 SER A CB  1 
ATOM   685  O  OG  . SER A 1 147 ? 32.925  8.405   7.093   1.00 22.72 ? 147 SER A OG  1 
ATOM   686  N  N   . LEU A 1 148 ? 35.732  6.485   6.610   1.00 21.55 ? 148 LEU A N   1 
ATOM   687  C  CA  . LEU A 1 148 ? 36.893  5.959   7.358   1.00 24.71 ? 148 LEU A CA  1 
ATOM   688  C  C   . LEU A 1 148 ? 38.193  6.008   6.522   1.00 24.36 ? 148 LEU A C   1 
ATOM   689  O  O   . LEU A 1 148 ? 39.290  6.076   7.070   1.00 22.94 ? 148 LEU A O   1 
ATOM   690  C  CB  . LEU A 1 148 ? 36.650  4.522   7.824   1.00 23.74 ? 148 LEU A CB  1 
ATOM   691  C  CG  . LEU A 1 148 ? 37.764  3.936   8.698   1.00 23.84 ? 148 LEU A CG  1 
ATOM   692  C  CD1 . LEU A 1 148 ? 37.721  4.581   10.036  1.00 26.10 ? 148 LEU A CD1 1 
ATOM   693  C  CD2 . LEU A 1 148 ? 37.683  2.407   8.774   1.00 27.46 ? 148 LEU A CD2 1 
ATOM   694  N  N   . PHE A 1 149 ? 38.075  5.828   5.205   1.00 24.95 ? 149 PHE A N   1 
ATOM   695  C  CA  . PHE A 1 149 ? 39.238  5.562   4.375   1.00 26.56 ? 149 PHE A CA  1 
ATOM   696  C  C   . PHE A 1 149 ? 40.002  6.874   4.086   1.00 30.82 ? 149 PHE A C   1 
ATOM   697  O  O   . PHE A 1 149 ? 41.084  6.854   3.538   1.00 33.11 ? 149 PHE A O   1 
ATOM   698  C  CB  . PHE A 1 149 ? 38.832  4.818   3.094   1.00 27.61 ? 149 PHE A CB  1 
ATOM   699  C  CG  . PHE A 1 149 ? 38.276  3.441   3.352   1.00 28.41 ? 149 PHE A CG  1 
ATOM   700  C  CD1 . PHE A 1 149 ? 36.926  3.252   3.633   1.00 27.05 ? 149 PHE A CD1 1 
ATOM   701  C  CD2 . PHE A 1 149 ? 39.126  2.341   3.357   1.00 28.34 ? 149 PHE A CD2 1 
ATOM   702  C  CE1 . PHE A 1 149 ? 36.443  1.986   3.921   1.00 26.62 ? 149 PHE A CE1 1 
ATOM   703  C  CE2 . PHE A 1 149 ? 38.639  1.073   3.620   1.00 26.64 ? 149 PHE A CE2 1 
ATOM   704  C  CZ  . PHE A 1 149 ? 37.312  0.914   3.954   1.00 28.37 ? 149 PHE A CZ  1 
ATOM   705  N  N   . THR A 1 150 ? 39.464  8.007   4.514   1.00 25.89 ? 150 THR A N   1 
ATOM   706  C  CA  . THR A 1 150 ? 40.215  9.254   4.509   1.00 31.71 ? 150 THR A CA  1 
ATOM   707  C  C   . THR A 1 150 ? 41.213  9.332   5.667   1.00 35.67 ? 150 THR A C   1 
ATOM   708  O  O   . THR A 1 150 ? 41.961  10.285  5.688   1.00 37.93 ? 150 THR A O   1 
ATOM   709  C  CB  . THR A 1 150 ? 39.284  10.467  4.519   1.00 32.39 ? 150 THR A CB  1 
ATOM   710  O  OG1 . THR A 1 150 ? 38.638  10.521  5.792   1.00 31.42 ? 150 THR A OG1 1 
ATOM   711  C  CG2 . THR A 1 150 ? 38.288  10.435  3.380   1.00 35.84 ? 150 THR A CG2 1 
ATOM   712  N  N   . ARG A 1 151 ? 41.258  8.324   6.570   1.00 35.30 ? 151 ARG A N   1 
ATOM   713  C  CA  . ARG A 1 151 ? 42.087  8.334   7.762   1.00 33.05 ? 151 ARG A CA  1 
ATOM   714  C  C   . ARG A 1 151 ? 43.101  7.202   7.669   1.00 33.31 ? 151 ARG A C   1 
ATOM   715  O  O   . ARG A 1 151 ? 42.901  6.275   6.891   1.00 29.18 ? 151 ARG A O   1 
ATOM   716  C  CB  . ARG A 1 151 ? 41.251  8.103   9.023   1.00 39.84 ? 151 ARG A CB  1 
ATOM   717  C  CG  . ARG A 1 151 ? 40.207  9.180   9.287   1.00 49.18 ? 151 ARG A CG  1 
ATOM   718  C  CD  . ARG A 1 151 ? 39.505  8.988   10.610  1.00 50.30 ? 151 ARG A CD  1 
ATOM   719  N  NE  . ARG A 1 151 ? 38.759  10.194  10.954  1.00 54.50 ? 151 ARG A NE  1 
ATOM   720  C  CZ  . ARG A 1 151 ? 39.188  11.106  11.817  1.00 55.58 ? 151 ARG A CZ  1 
ATOM   721  N  NH1 . ARG A 1 151 ? 40.100  10.822  12.728  1.00 45.06 ? 151 ARG A NH1 1 
ATOM   722  N  NH2 . ARG A 1 151 ? 38.675  12.315  11.784  1.00 65.03 ? 151 ARG A NH2 1 
ATOM   723  N  N   . PHE A 1 152 ? 44.157  7.278   8.512   1.00 27.98 ? 152 PHE A N   1 
ATOM   724  C  CA  . PHE A 1 152 ? 45.063  6.161   8.815   1.00 31.92 ? 152 PHE A CA  1 
ATOM   725  C  C   . PHE A 1 152 ? 45.755  5.600   7.571   1.00 31.98 ? 152 PHE A C   1 
ATOM   726  O  O   . PHE A 1 152 ? 46.202  4.449   7.585   1.00 35.98 ? 152 PHE A O   1 
ATOM   727  C  CB  . PHE A 1 152 ? 44.354  4.968   9.484   1.00 31.47 ? 152 PHE A CB  1 
ATOM   728  C  CG  . PHE A 1 152 ? 43.483  5.348   10.650  1.00 30.25 ? 152 PHE A CG  1 
ATOM   729  C  CD1 . PHE A 1 152 ? 43.983  6.153   11.650  1.00 30.59 ? 152 PHE A CD1 1 
ATOM   730  C  CD2 . PHE A 1 152 ? 42.173  4.895   10.755  1.00 32.66 ? 152 PHE A CD2 1 
ATOM   731  C  CE1 . PHE A 1 152 ? 43.196  6.478   12.733  1.00 28.66 ? 152 PHE A CE1 1 
ATOM   732  C  CE2 . PHE A 1 152 ? 41.383  5.271   11.826  1.00 30.78 ? 152 PHE A CE2 1 
ATOM   733  C  CZ  . PHE A 1 152 ? 41.922  6.012   12.843  1.00 30.67 ? 152 PHE A CZ  1 
ATOM   734  N  N   . GLY A 1 153 ? 45.840  6.415   6.513   1.00 30.77 ? 153 GLY A N   1 
ATOM   735  C  CA  . GLY A 1 153 ? 46.525  6.013   5.313   1.00 27.41 ? 153 GLY A CA  1 
ATOM   736  C  C   . GLY A 1 153 ? 45.779  4.965   4.501   1.00 35.23 ? 153 GLY A C   1 
ATOM   737  O  O   . GLY A 1 153 ? 46.388  4.240   3.716   1.00 31.08 ? 153 GLY A O   1 
ATOM   738  N  N   . LEU A 1 154 ? 44.450  4.922   4.652   1.00 30.71 ? 154 LEU A N   1 
ATOM   739  C  CA  . LEU A 1 154 ? 43.667  3.851   4.072   1.00 32.41 ? 154 LEU A CA  1 
ATOM   740  C  C   . LEU A 1 154 ? 43.080  4.187   2.701   1.00 28.70 ? 154 LEU A C   1 
ATOM   741  O  O   . LEU A 1 154 ? 42.324  3.374   2.188   1.00 31.27 ? 154 LEU A O   1 
ATOM   742  C  CB  . LEU A 1 154 ? 42.507  3.554   5.040   1.00 27.35 ? 154 LEU A CB  1 
ATOM   743  C  CG  . LEU A 1 154 ? 42.891  2.925   6.370   1.00 32.11 ? 154 LEU A CG  1 
ATOM   744  C  CD1 . LEU A 1 154 ? 41.629  2.780   7.215   1.00 31.49 ? 154 LEU A CD1 1 
ATOM   745  C  CD2 . LEU A 1 154 ? 43.641  1.591   6.181   1.00 32.81 ? 154 LEU A CD2 1 
ATOM   746  N  N   . ALA A 1 155 ? 43.364  5.370   2.121   1.00 28.84 ? 155 ALA A N   1 
ATOM   747  C  CA  . ALA A 1 155 ? 42.643  5.837   0.931   1.00 31.85 ? 155 ALA A CA  1 
ATOM   748  C  C   . ALA A 1 155 ? 42.625  4.825   -0.219  1.00 32.04 ? 155 ALA A C   1 
ATOM   749  O  O   . ALA A 1 155 ? 41.596  4.619   -0.862  1.00 29.14 ? 155 ALA A O   1 
ATOM   750  C  CB  . ALA A 1 155 ? 43.220  7.160   0.459   1.00 36.92 ? 155 ALA A CB  1 
ATOM   751  N  N   . ASP A 1 156 ? 43.747  4.161   -0.482  1.00 31.55 ? 156 ASP A N   1 
ATOM   752  C  CA  . ASP A 1 156 ? 43.821  3.247   -1.618  1.00 33.20 ? 156 ASP A CA  1 
ATOM   753  C  C   . ASP A 1 156 ? 43.189  1.881   -1.326  1.00 31.32 ? 156 ASP A C   1 
ATOM   754  O  O   . ASP A 1 156 ? 43.116  1.042   -2.218  1.00 28.02 ? 156 ASP A O   1 
ATOM   755  C  CB  . ASP A 1 156 ? 45.269  2.888   -1.968  1.00 37.93 ? 156 ASP A CB  1 
ATOM   756  C  CG  . ASP A 1 156 ? 46.119  4.076   -2.370  1.00 42.48 ? 156 ASP A CG  1 
ATOM   757  O  OD1 . ASP A 1 156 ? 45.566  5.023   -2.977  1.00 38.19 ? 156 ASP A OD1 1 
ATOM   758  O  OD2 . ASP A 1 156 ? 47.331  4.007   -2.105  1.00 54.98 ? 156 ASP A OD2 1 
ATOM   759  N  N   . LEU A 1 157 ? 42.752  1.652   -0.086  1.00 28.74 ? 157 LEU A N   1 
ATOM   760  C  CA  . LEU A 1 157 ? 42.198  0.349   0.231   1.00 28.70 ? 157 LEU A CA  1 
ATOM   761  C  C   . LEU A 1 157 ? 40.669  0.403   0.223   1.00 26.75 ? 157 LEU A C   1 
ATOM   762  O  O   . LEU A 1 157 ? 40.052  -0.626  0.459   1.00 28.85 ? 157 LEU A O   1 
ATOM   763  C  CB  . LEU A 1 157 ? 42.751  -0.090  1.590   1.00 29.41 ? 157 LEU A CB  1 
ATOM   764  C  CG  . LEU A 1 157 ? 44.211  -0.506  1.553   1.00 32.83 ? 157 LEU A CG  1 
ATOM   765  C  CD1 . LEU A 1 157 ? 44.748  -0.714  2.959   1.00 35.30 ? 157 LEU A CD1 1 
ATOM   766  C  CD2 . LEU A 1 157 ? 44.352  -1.753  0.736   1.00 31.11 ? 157 LEU A CD2 1 
ATOM   767  N  N   . ARG A 1 158 ? 40.089  1.560   -0.086  1.00 24.24 ? 158 ARG A N   1 
ATOM   768  C  CA  . ARG A 1 158 ? 38.638  1.657   -0.195  1.00 25.81 ? 158 ARG A CA  1 
ATOM   769  C  C   . ARG A 1 158 ? 38.157  0.750   -1.329  1.00 24.48 ? 158 ARG A C   1 
ATOM   770  O  O   . ARG A 1 158 ? 38.573  0.946   -2.482  1.00 25.50 ? 158 ARG A O   1 
ATOM   771  C  CB  . ARG A 1 158 ? 38.159  3.058   -0.505  1.00 22.90 ? 158 ARG A CB  1 
ATOM   772  C  CG  . ARG A 1 158 ? 36.632  3.132   -0.580  1.00 27.17 ? 158 ARG A CG  1 
ATOM   773  C  CD  . ARG A 1 158 ? 36.201  4.532   -0.952  1.00 30.10 ? 158 ARG A CD  1 
ATOM   774  N  NE  . ARG A 1 158 ? 34.784  4.520   -1.319  1.00 30.13 ? 158 ARG A NE  1 
ATOM   775  C  CZ  . ARG A 1 158 ? 34.009  5.608   -1.341  1.00 28.46 ? 158 ARG A CZ  1 
ATOM   776  N  NH1 . ARG A 1 158 ? 34.557  6.779   -1.109  1.00 31.55 ? 158 ARG A NH1 1 
ATOM   777  N  NH2 . ARG A 1 158 ? 32.694  5.485   -1.487  1.00 24.67 ? 158 ARG A NH2 1 
ATOM   778  N  N   . PRO A 1 159 ? 37.293  -0.259  -1.044  1.00 25.67 ? 159 PRO A N   1 
ATOM   779  C  CA  . PRO A 1 159 ? 36.741  -1.092  -2.100  1.00 24.30 ? 159 PRO A CA  1 
ATOM   780  C  C   . PRO A 1 159 ? 35.921  -0.279  -3.103  1.00 23.18 ? 159 PRO A C   1 
ATOM   781  O  O   . PRO A 1 159 ? 35.070  0.546   -2.759  1.00 21.78 ? 159 PRO A O   1 
ATOM   782  C  CB  . PRO A 1 159 ? 35.819  -2.078  -1.338  1.00 24.35 ? 159 PRO A CB  1 
ATOM   783  C  CG  . PRO A 1 159 ? 36.218  -1.965  0.125   1.00 25.48 ? 159 PRO A CG  1 
ATOM   784  C  CD  . PRO A 1 159 ? 36.692  -0.543  0.287   1.00 22.07 ? 159 PRO A CD  1 
ATOM   785  N  N   . GLU A 1 160 ? 36.084  -0.622  -4.382  1.00 23.84 ? 160 GLU A N   1 
ATOM   786  C  CA  . GLU A 1 160 ? 35.242  -0.118  -5.434  1.00 27.66 ? 160 GLU A CA  1 
ATOM   787  C  C   . GLU A 1 160 ? 33.770  -0.502  -5.176  1.00 23.07 ? 160 GLU A C   1 
ATOM   788  O  O   . GLU A 1 160 ? 32.874  0.247   -5.534  1.00 22.64 ? 160 GLU A O   1 
ATOM   789  C  CB  . GLU A 1 160 ? 35.784  -0.657  -6.764  1.00 33.40 ? 160 GLU A CB  1 
ATOM   790  C  CG  . GLU A 1 160 ? 36.951  0.175   -7.231  1.00 44.56 ? 160 GLU A CG  1 
ATOM   791  C  CD  . GLU A 1 160 ? 36.477  1.180   -8.262  1.00 47.82 ? 160 GLU A CD  1 
ATOM   792  O  OE1 . GLU A 1 160 ? 36.131  0.747   -9.383  1.00 58.75 ? 160 GLU A OE1 1 
ATOM   793  O  OE2 . GLU A 1 160 ? 36.414  2.361   -7.935  1.00 50.21 ? 160 GLU A OE2 1 
ATOM   794  N  N   . ALA A 1 161 ? 33.490  -1.641  -4.531  1.00 20.37 ? 161 ALA A N   1 
ATOM   795  C  CA  . ALA A 1 161 ? 32.115  -2.054  -4.360  1.00 21.19 ? 161 ALA A CA  1 
ATOM   796  C  C   . ALA A 1 161 ? 31.432  -1.168  -3.309  1.00 20.61 ? 161 ALA A C   1 
ATOM   797  O  O   . ALA A 1 161 ? 30.214  -1.263  -3.117  1.00 24.04 ? 161 ALA A O   1 
ATOM   798  C  CB  . ALA A 1 161 ? 32.086  -3.517  -3.982  1.00 20.53 ? 161 ALA A CB  1 
ATOM   799  N  N   . LEU A 1 162 ? 32.239  -0.417  -2.523  1.00 21.14 ? 162 LEU A N   1 
ATOM   800  C  CA  . LEU A 1 162 ? 31.730  0.472   -1.497  1.00 20.79 ? 162 LEU A CA  1 
ATOM   801  C  C   . LEU A 1 162 ? 31.464  1.808   -2.170  1.00 24.80 ? 162 LEU A C   1 
ATOM   802  O  O   . LEU A 1 162 ? 32.230  2.769   -2.008  1.00 26.19 ? 162 LEU A O   1 
ATOM   803  C  CB  . LEU A 1 162 ? 32.727  0.603   -0.337  1.00 19.98 ? 162 LEU A CB  1 
ATOM   804  C  CG  . LEU A 1 162 ? 32.226  1.471   0.838   1.00 20.32 ? 162 LEU A CG  1 
ATOM   805  C  CD1 . LEU A 1 162 ? 30.914  0.978   1.430   1.00 21.76 ? 162 LEU A CD1 1 
ATOM   806  C  CD2 . LEU A 1 162 ? 33.235  1.573   1.937   1.00 21.54 ? 162 LEU A CD2 1 
ATOM   807  N  N   . ALA A 1 163 ? 30.390  1.813   -2.957  1.00 26.92 ? 163 ALA A N   1 
ATOM   808  C  CA  . ALA A 1 163 ? 30.032  2.945   -3.815  1.00 27.89 ? 163 ALA A CA  1 
ATOM   809  C  C   . ALA A 1 163 ? 29.231  3.949   -2.998  1.00 26.73 ? 163 ALA A C   1 
ATOM   810  O  O   . ALA A 1 163 ? 28.344  3.562   -2.232  1.00 26.35 ? 163 ALA A O   1 
ATOM   811  C  CB  . ALA A 1 163 ? 29.196  2.421   -4.993  1.00 26.82 ? 163 ALA A CB  1 
ATOM   812  N  N   . ASP A 1 164 ? 29.433  5.236   -3.262  1.00 27.89 ? 164 ASP A N   1 
ATOM   813  C  CA  . ASP A 1 164 ? 28.481  6.224   -2.773  1.00 25.18 ? 164 ASP A CA  1 
ATOM   814  C  C   . ASP A 1 164 ? 27.170  6.077   -3.535  1.00 27.45 ? 164 ASP A C   1 
ATOM   815  O  O   . ASP A 1 164 ? 27.165  5.811   -4.729  1.00 31.76 ? 164 ASP A O   1 
ATOM   816  C  CB  . ASP A 1 164 ? 28.992  7.628   -2.943  1.00 27.02 ? 164 ASP A CB  1 
ATOM   817  C  CG  . ASP A 1 164 ? 30.236  7.880   -2.110  1.00 34.38 ? 164 ASP A CG  1 
ATOM   818  O  OD1 . ASP A 1 164 ? 30.281  7.467   -0.946  1.00 39.60 ? 164 ASP A OD1 1 
ATOM   819  O  OD2 . ASP A 1 164 ? 31.125  8.515   -2.642  1.00 48.48 ? 164 ASP A OD2 1 
ATOM   820  N  N   . LEU A 1 165 ? 26.054  6.229   -2.814  1.00 22.90 ? 165 LEU A N   1 
ATOM   821  C  CA  . LEU A 1 165 ? 24.769  6.125   -3.463  1.00 23.42 ? 165 LEU A CA  1 
ATOM   822  C  C   . LEU A 1 165 ? 24.509  7.410   -4.260  1.00 25.11 ? 165 LEU A C   1 
ATOM   823  O  O   . LEU A 1 165 ? 24.813  8.496   -3.808  1.00 27.95 ? 165 LEU A O   1 
ATOM   824  C  CB  . LEU A 1 165 ? 23.697  5.887   -2.408  1.00 22.36 ? 165 LEU A CB  1 
ATOM   825  C  CG  . LEU A 1 165 ? 23.832  4.580   -1.629  1.00 20.84 ? 165 LEU A CG  1 
ATOM   826  C  CD1 . LEU A 1 165 ? 22.723  4.464   -0.607  1.00 20.36 ? 165 LEU A CD1 1 
ATOM   827  C  CD2 . LEU A 1 165 ? 23.856  3.405   -2.505  1.00 19.88 ? 165 LEU A CD2 1 
ATOM   828  N  N   . PRO A 1 166 ? 23.828  7.305   -5.396  1.00 26.31 ? 166 PRO A N   1 
ATOM   829  C  CA  . PRO A 1 166 ? 23.326  8.499   -6.099  1.00 29.02 ? 166 PRO A CA  1 
ATOM   830  C  C   . PRO A 1 166 ? 22.141  9.055   -5.333  1.00 29.64 ? 166 PRO A C   1 
ATOM   831  O  O   . PRO A 1 166 ? 21.615  8.378   -4.437  1.00 26.25 ? 166 PRO A O   1 
ATOM   832  C  CB  . PRO A 1 166 ? 22.906  7.932   -7.464  1.00 30.31 ? 166 PRO A CB  1 
ATOM   833  C  CG  . PRO A 1 166 ? 22.572  6.460   -7.217  1.00 30.90 ? 166 PRO A CG  1 
ATOM   834  C  CD  . PRO A 1 166 ? 23.458  6.026   -6.057  1.00 25.79 ? 166 PRO A CD  1 
ATOM   835  N  N   . LYS A 1 167 ? 21.710  10.271  -5.690  1.00 26.42 ? 167 LYS A N   1 
ATOM   836  C  CA  . LYS A 1 167 ? 20.478  10.851  -5.145  1.00 27.59 ? 167 LYS A CA  1 
ATOM   837  C  C   . LYS A 1 167 ? 19.329  10.197  -5.882  1.00 25.29 ? 167 LYS A C   1 
ATOM   838  O  O   . LYS A 1 167 ? 19.388  10.026  -7.088  1.00 26.49 ? 167 LYS A O   1 
ATOM   839  C  CB  . LYS A 1 167 ? 20.366  12.364  -5.374  1.00 38.49 ? 167 LYS A CB  1 
ATOM   840  N  N   . PHE A 1 168 ? 18.337  9.757   -5.145  1.00 23.23 ? 168 PHE A N   1 
ATOM   841  C  CA  . PHE A 1 168 ? 17.175  9.129   -5.741  1.00 25.32 ? 168 PHE A CA  1 
ATOM   842  C  C   . PHE A 1 168 ? 16.031  10.143  -5.653  1.00 23.32 ? 168 PHE A C   1 
ATOM   843  O  O   . PHE A 1 168 ? 15.854  10.835  -4.649  1.00 21.30 ? 168 PHE A O   1 
ATOM   844  C  CB  . PHE A 1 168 ? 16.796  7.787   -5.082  1.00 21.39 ? 168 PHE A CB  1 
ATOM   845  C  CG  . PHE A 1 168 ? 17.843  6.718   -5.202  1.00 19.40 ? 168 PHE A CG  1 
ATOM   846  C  CD1 . PHE A 1 168 ? 18.051  6.061   -6.413  1.00 21.35 ? 168 PHE A CD1 1 
ATOM   847  C  CD2 . PHE A 1 168 ? 18.699  6.437   -4.136  1.00 18.05 ? 168 PHE A CD2 1 
ATOM   848  C  CE1 . PHE A 1 168 ? 19.081  5.152   -6.547  1.00 24.06 ? 168 PHE A CE1 1 
ATOM   849  C  CE2 . PHE A 1 168 ? 19.694  5.491   -4.282  1.00 20.69 ? 168 PHE A CE2 1 
ATOM   850  C  CZ  . PHE A 1 168 ? 19.897  4.857   -5.464  1.00 24.08 ? 168 PHE A CZ  1 
ATOM   851  N  N   . PRO A 1 169 ? 15.122  10.149  -6.637  1.00 26.10 ? 169 PRO A N   1 
ATOM   852  C  CA  . PRO A 1 169 ? 13.933  10.997  -6.512  1.00 27.57 ? 169 PRO A CA  1 
ATOM   853  C  C   . PRO A 1 169 ? 13.152  10.745  -5.226  1.00 28.35 ? 169 PRO A C   1 
ATOM   854  O  O   . PRO A 1 169 ? 12.964  9.609   -4.809  1.00 29.35 ? 169 PRO A O   1 
ATOM   855  C  CB  . PRO A 1 169 ? 13.062  10.572  -7.697  1.00 30.52 ? 169 PRO A CB  1 
ATOM   856  C  CG  . PRO A 1 169 ? 14.010  9.893   -8.655  1.00 31.81 ? 169 PRO A CG  1 
ATOM   857  C  CD  . PRO A 1 169 ? 15.159  9.324   -7.847  1.00 26.45 ? 169 PRO A CD  1 
ATOM   858  N  N   . GLY A 1 170 ? 12.760  11.810  -4.553  1.00 24.77 ? 170 GLY A N   1 
ATOM   859  C  CA  . GLY A 1 170 ? 11.959  11.743  -3.343  1.00 27.21 ? 170 GLY A CA  1 
ATOM   860  C  C   . GLY A 1 170 ? 12.791  11.662  -2.049  1.00 25.93 ? 170 GLY A C   1 
ATOM   861  O  O   . GLY A 1 170 ? 12.211  11.869  -0.980  1.00 24.87 ? 170 GLY A O   1 
ATOM   862  N  N   . ASP A 1 171 ? 14.116  11.408  -2.154  1.00 28.00 ? 171 ASP A N   1 
ATOM   863  C  CA  . ASP A 1 171 ? 15.072  11.455  -1.032  1.00 24.63 ? 171 ASP A CA  1 
ATOM   864  C  C   . ASP A 1 171 ? 14.863  12.742  -0.249  1.00 26.99 ? 171 ASP A C   1 
ATOM   865  O  O   . ASP A 1 171 ? 14.826  13.852  -0.822  1.00 21.06 ? 171 ASP A O   1 
ATOM   866  C  CB  . ASP A 1 171 ? 16.557  11.481  -1.487  1.00 23.61 ? 171 ASP A CB  1 
ATOM   867  C  CG  . ASP A 1 171 ? 17.274  10.163  -1.810  1.00 25.65 ? 171 ASP A CG  1 
ATOM   868  O  OD1 . ASP A 1 171 ? 16.637  9.098   -1.646  1.00 22.27 ? 171 ASP A OD1 1 
ATOM   869  O  OD2 . ASP A 1 171 ? 18.489  10.227  -2.288  1.00 29.60 ? 171 ASP A OD2 1 
ATOM   870  N  N   . ASN A 1 172 ? 14.845  12.608  1.068   1.00 19.81 ? 172 ASN A N   1 
ATOM   871  C  CA  . ASN A 1 172 ? 14.925  13.751  1.967   1.00 21.17 ? 172 ASN A CA  1 
ATOM   872  C  C   . ASN A 1 172 ? 15.822  13.372  3.145   1.00 19.88 ? 172 ASN A C   1 
ATOM   873  O  O   . ASN A 1 172 ? 15.327  13.180  4.245   1.00 17.95 ? 172 ASN A O   1 
ATOM   874  C  CB  . ASN A 1 172 ? 13.564  14.222  2.402   1.00 24.48 ? 172 ASN A CB  1 
ATOM   875  C  CG  . ASN A 1 172 ? 13.610  15.546  3.127   1.00 32.99 ? 172 ASN A CG  1 
ATOM   876  O  OD1 . ASN A 1 172 ? 14.603  16.250  3.041   1.00 39.02 ? 172 ASN A OD1 1 
ATOM   877  N  ND2 . ASN A 1 172 ? 12.576  15.856  3.873   1.00 36.29 ? 172 ASN A ND2 1 
ATOM   878  N  N   . LEU A 1 173 ? 17.119  13.262  2.892   1.00 20.75 ? 173 LEU A N   1 
ATOM   879  C  CA  . LEU A 1 173 ? 18.041  12.658  3.851   1.00 22.61 ? 173 LEU A CA  1 
ATOM   880  C  C   . LEU A 1 173 ? 18.436  13.688  4.913   1.00 22.71 ? 173 LEU A C   1 
ATOM   881  O  O   . LEU A 1 173 ? 18.766  14.823  4.627   1.00 26.53 ? 173 LEU A O   1 
ATOM   882  C  CB  . LEU A 1 173 ? 19.290  12.089  3.153   1.00 22.93 ? 173 LEU A CB  1 
ATOM   883  C  CG  . LEU A 1 173 ? 19.026  11.140  1.979   1.00 22.84 ? 173 LEU A CG  1 
ATOM   884  C  CD1 . LEU A 1 173 ? 20.305  10.603  1.356   1.00 24.88 ? 173 LEU A CD1 1 
ATOM   885  C  CD2 . LEU A 1 173 ? 18.143  9.994   2.450   1.00 25.00 ? 173 LEU A CD2 1 
ATOM   886  N  N   . ASP A 1 174 ? 18.278  13.315  6.162   1.00 23.18 ? 174 ASP A N   1 
ATOM   887  C  CA  . ASP A 1 174 ? 18.858  14.052  7.274   1.00 24.44 ? 174 ASP A CA  1 
ATOM   888  C  C   . ASP A 1 174 ? 20.356  13.713  7.387   1.00 25.96 ? 174 ASP A C   1 
ATOM   889  O  O   . ASP A 1 174 ? 20.723  12.604  7.738   1.00 20.21 ? 174 ASP A O   1 
ATOM   890  C  CB  . ASP A 1 174 ? 18.014  13.756  8.501   1.00 27.53 ? 174 ASP A CB  1 
ATOM   891  C  CG  . ASP A 1 174 ? 18.495  14.454  9.759   1.00 33.64 ? 174 ASP A CG  1 
ATOM   892  O  OD1 . ASP A 1 174 ? 19.551  15.066  9.751   1.00 32.43 ? 174 ASP A OD1 1 
ATOM   893  O  OD2 . ASP A 1 174 ? 17.789  14.365  10.684  1.00 32.41 ? 174 ASP A OD2 1 
ATOM   894  N  N   . ARG A 1 175 ? 21.227  14.715  7.151   1.00 25.34 ? 175 ARG A N   1 
ATOM   895  C  CA  . ARG A 1 175 ? 22.670  14.550  7.159   1.00 26.09 ? 175 ARG A CA  1 
ATOM   896  C  C   . ARG A 1 175 ? 23.147  14.060  8.533   1.00 24.79 ? 175 ARG A C   1 
ATOM   897  O  O   . ARG A 1 175 ? 24.115  13.277  8.570   1.00 27.37 ? 175 ARG A O   1 
ATOM   898  C  CB  . ARG A 1 175 ? 23.363  15.866  6.724   1.00 29.04 ? 175 ARG A CB  1 
ATOM   899  C  CG  . ARG A 1 175 ? 23.516  16.027  5.210   1.00 39.32 ? 175 ARG A CG  1 
ATOM   900  N  N   . ALA A 1 176 ? 22.431  14.370  9.622   1.00 28.99 ? 176 ALA A N   1 
ATOM   901  C  CA  . ALA A 1 176 ? 22.862  14.015  10.976  1.00 32.93 ? 176 ALA A CA  1 
ATOM   902  C  C   . ALA A 1 176 ? 22.637  12.530  11.218  1.00 31.63 ? 176 ALA A C   1 
ATOM   903  O  O   . ALA A 1 176 ? 23.275  11.926  12.087  1.00 32.73 ? 176 ALA A O   1 
ATOM   904  C  CB  . ALA A 1 176 ? 22.085  14.744  12.023  1.00 31.40 ? 176 ALA A CB  1 
ATOM   905  N  N   . ARG A 1 177 ? 21.622  11.998  10.550  1.00 23.81 ? 177 ARG A N   1 
ATOM   906  C  CA  . ARG A 1 177 ? 21.267  10.598  10.719  1.00 28.49 ? 177 ARG A CA  1 
ATOM   907  C  C   . ARG A 1 177 ? 21.621  9.756   9.499   1.00 23.37 ? 177 ARG A C   1 
ATOM   908  O  O   . ARG A 1 177 ? 20.899  8.792   9.168   1.00 24.05 ? 177 ARG A O   1 
ATOM   909  C  CB  . ARG A 1 177 ? 19.781  10.454  10.983  1.00 30.58 ? 177 ARG A CB  1 
ATOM   910  C  CG  . ARG A 1 177 ? 19.375  10.883  12.380  1.00 42.31 ? 177 ARG A CG  1 
ATOM   911  C  CD  . ARG A 1 177 ? 18.151  10.015  12.520  1.00 46.20 ? 177 ARG A CD  1 
ATOM   912  N  NE  . ARG A 1 177 ? 17.501  10.185  13.783  1.00 48.48 ? 177 ARG A NE  1 
ATOM   913  C  CZ  . ARG A 1 177 ? 16.893  9.211   14.412  1.00 49.89 ? 177 ARG A CZ  1 
ATOM   914  N  NH1 . ARG A 1 177 ? 15.771  9.462   15.071  1.00 58.31 ? 177 ARG A NH1 1 
ATOM   915  N  NH2 . ARG A 1 177 ? 17.408  7.994   14.338  1.00 50.28 ? 177 ARG A NH2 1 
ATOM   916  N  N   . SER A 1 178 ? 22.707  10.175  8.833   1.00 17.40 ? 178 SER A N   1 
ATOM   917  C  CA  . SER A 1 178 ? 23.246  9.572   7.634   1.00 17.20 ? 178 SER A CA  1 
ATOM   918  C  C   . SER A 1 178 ? 24.753  9.436   7.834   1.00 18.80 ? 178 SER A C   1 
ATOM   919  O  O   . SER A 1 178 ? 25.339  10.173  8.649   1.00 18.37 ? 178 SER A O   1 
ATOM   920  C  CB  . SER A 1 178 ? 22.941  10.392  6.402   1.00 18.67 ? 178 SER A CB  1 
ATOM   921  O  OG  . SER A 1 178 ? 21.527  10.440  6.194   1.00 18.85 ? 178 SER A OG  1 
ATOM   922  N  N   . GLY A 1 179 ? 25.322  8.516   7.087   1.00 20.36 ? 179 GLY A N   1 
ATOM   923  C  CA  . GLY A 1 179 ? 26.762  8.352   7.043   1.00 20.02 ? 179 GLY A CA  1 
ATOM   924  C  C   . GLY A 1 179 ? 27.311  7.745   8.318   1.00 20.70 ? 179 GLY A C   1 
ATOM   925  O  O   . GLY A 1 179 ? 26.598  7.052   9.037   1.00 19.54 ? 179 GLY A O   1 
ATOM   926  N  N   . GLY A 1 180 ? 28.579  8.006   8.577   1.00 17.91 ? 180 GLY A N   1 
ATOM   927  C  CA  . GLY A 1 180 ? 29.246  7.380   9.714   1.00 18.37 ? 180 GLY A CA  1 
ATOM   928  C  C   . GLY A 1 180 ? 30.511  6.709   9.234   1.00 17.55 ? 180 GLY A C   1 
ATOM   929  O  O   . GLY A 1 180 ? 30.491  5.933   8.275   1.00 19.71 ? 180 GLY A O   1 
ATOM   930  N  N   . ASP A 1 181 ? 31.574  6.857   10.039  1.00 17.80 ? 181 ASP A N   1 
ATOM   931  C  CA  . ASP A 1 181 ? 32.811  6.178   9.768   1.00 16.43 ? 181 ASP A CA  1 
ATOM   932  C  C   . ASP A 1 181 ? 32.712  4.680   9.996   1.00 15.61 ? 181 ASP A C   1 
ATOM   933  O  O   . ASP A 1 181 ? 33.428  3.914   9.329   1.00 16.77 ? 181 ASP A O   1 
ATOM   934  C  CB  . ASP A 1 181 ? 33.940  6.677   10.665  1.00 18.32 ? 181 ASP A CB  1 
ATOM   935  C  CG  . ASP A 1 181 ? 34.380  8.115   10.355  1.00 23.71 ? 181 ASP A CG  1 
ATOM   936  O  OD1 . ASP A 1 181 ? 34.117  8.605   9.247   1.00 22.42 ? 181 ASP A OD1 1 
ATOM   937  O  OD2 . ASP A 1 181 ? 34.861  8.762   11.286  1.00 21.42 ? 181 ASP A OD2 1 
ATOM   938  N  N   . LEU A 1 182 ? 31.920  4.255   10.975  1.00 17.29 ? 182 LEU A N   1 
ATOM   939  C  CA  . LEU A 1 182 ? 31.710  2.821   11.156  1.00 20.73 ? 182 LEU A CA  1 
ATOM   940  C  C   . LEU A 1 182 ? 30.381  2.532   11.816  1.00 16.14 ? 182 LEU A C   1 
ATOM   941  O  O   . LEU A 1 182 ? 29.718  3.423   12.238  1.00 17.38 ? 182 LEU A O   1 
ATOM   942  C  CB  . LEU A 1 182 ? 32.856  2.196   11.944  1.00 30.38 ? 182 LEU A CB  1 
ATOM   943  C  CG  . LEU A 1 182 ? 32.991  2.637   13.378  1.00 30.49 ? 182 LEU A CG  1 
ATOM   944  C  CD1 . LEU A 1 182 ? 32.400  1.570   14.274  1.00 40.92 ? 182 LEU A CD1 1 
ATOM   945  C  CD2 . LEU A 1 182 ? 34.427  2.847   13.766  1.00 43.83 ? 182 LEU A CD2 1 
ATOM   946  N  N   . CYS A 1 183 ? 29.965  1.264   11.804  1.00 14.71 ? 183 CYS A N   1 
ATOM   947  C  CA  . CYS A 1 183 ? 28.713  0.848   12.387  1.00 14.18 ? 183 CYS A CA  1 
ATOM   948  C  C   . CYS A 1 183 ? 28.888  -0.432  13.172  1.00 13.51 ? 183 CYS A C   1 
ATOM   949  O  O   . CYS A 1 183 ? 29.785  -1.229  12.914  1.00 15.33 ? 183 CYS A O   1 
ATOM   950  C  CB  . CYS A 1 183 ? 27.654  0.660   11.299  1.00 15.59 ? 183 CYS A CB  1 
ATOM   951  S  SG  . CYS A 1 183 ? 27.863  -0.773  10.260  1.00 17.39 ? 183 CYS A SG  1 
ATOM   952  N  N   . VAL A 1 184 ? 28.028  -0.566  14.185  1.00 14.31 ? 184 VAL A N   1 
ATOM   953  C  CA  . VAL A 1 184 ? 27.869  -1.833  14.850  1.00 13.51 ? 184 VAL A CA  1 
ATOM   954  C  C   . VAL A 1 184 ? 26.379  -2.127  14.830  1.00 13.28 ? 184 VAL A C   1 
ATOM   955  O  O   . VAL A 1 184 ? 25.574  -1.351  15.312  1.00 15.02 ? 184 VAL A O   1 
ATOM   956  C  CB  . VAL A 1 184 ? 28.436  -1.824  16.281  1.00 15.78 ? 184 VAL A CB  1 
ATOM   957  C  CG1 . VAL A 1 184 ? 28.205  -3.176  16.921  1.00 17.65 ? 184 VAL A CG1 1 
ATOM   958  C  CG2 . VAL A 1 184 ? 29.902  -1.512  16.236  1.00 17.35 ? 184 VAL A CG2 1 
ATOM   959  N  N   . GLN A 1 185 ? 26.024  -3.252  14.178  1.00 12.07 ? 185 GLN A N   1 
ATOM   960  C  CA  . GLN A 1 185 ? 24.683  -3.751  14.184  1.00 10.72 ? 185 GLN A CA  1 
ATOM   961  C  C   . GLN A 1 185 ? 24.589  -4.763  15.307  1.00 11.02 ? 185 GLN A C   1 
ATOM   962  O  O   . GLN A 1 185 ? 25.265  -5.777  15.282  1.00 12.66 ? 185 GLN A O   1 
ATOM   963  C  CB  . GLN A 1 185 ? 24.422  -4.441  12.835  1.00 11.40 ? 185 GLN A CB  1 
ATOM   964  C  CG  . GLN A 1 185 ? 23.077  -5.153  12.767  1.00 10.77 ? 185 GLN A CG  1 
ATOM   965  C  CD  . GLN A 1 185 ? 22.947  -6.046  11.555  1.00 13.53 ? 185 GLN A CD  1 
ATOM   966  O  OE1 . GLN A 1 185 ? 22.591  -5.559  10.475  1.00 13.63 ? 185 GLN A OE1 1 
ATOM   967  N  NE2 . GLN A 1 185 ? 23.310  -7.322  11.713  1.00 12.84 ? 185 GLN A NE2 1 
ATOM   968  N  N   . ALA A 1 186 ? 23.748  -4.472  16.319  1.00 11.22 ? 186 ALA A N   1 
ATOM   969  C  CA  . ALA A 1 186 ? 23.537  -5.420  17.406  1.00 11.65 ? 186 ALA A CA  1 
ATOM   970  C  C   . ALA A 1 186 ? 22.128  -5.967  17.283  1.00 12.82 ? 186 ALA A C   1 
ATOM   971  O  O   . ALA A 1 186 ? 21.166  -5.237  17.313  1.00 15.66 ? 186 ALA A O   1 
ATOM   972  C  CB  . ALA A 1 186 ? 23.749  -4.802  18.750  1.00 12.12 ? 186 ALA A CB  1 
ATOM   973  N  N   . CYS A 1 187 ? 22.024  -7.279  17.089  1.00 11.77 ? 187 CYS A N   1 
ATOM   974  C  CA  . CYS A 1 187 ? 20.724  -7.905  16.965  1.00 13.80 ? 187 CYS A CA  1 
ATOM   975  C  C   . CYS A 1 187 ? 20.636  -8.947  18.073  1.00 14.90 ? 187 CYS A C   1 
ATOM   976  O  O   . CYS A 1 187 ? 21.581  -9.688  18.300  1.00 15.08 ? 187 CYS A O   1 
ATOM   977  C  CB  . CYS A 1 187 ? 20.598  -8.657  15.649  1.00 14.21 ? 187 CYS A CB  1 
ATOM   978  S  SG  . CYS A 1 187 ? 20.576  -7.513  14.221  1.00 14.55 ? 187 CYS A SG  1 
ATOM   979  N  N   . ALA A 1 188 ? 19.483  -9.029  18.720  1.00 14.83 ? 188 ALA A N   1 
ATOM   980  C  CA  . ALA A 1 188 ? 19.303  -9.994  19.783  1.00 11.70 ? 188 ALA A CA  1 
ATOM   981  C  C   . ALA A 1 188 ? 17.797  -10.180 19.983  1.00 14.72 ? 188 ALA A C   1 
ATOM   982  O  O   . ALA A 1 188 ? 17.035  -9.365  19.521  1.00 14.94 ? 188 ALA A O   1 
ATOM   983  C  CB  . ALA A 1 188 ? 19.989  -9.515  20.993  1.00 11.87 ? 188 ALA A CB  1 
ATOM   984  N  N   . ASP A 1 189 ? 17.419  -11.215 20.720  1.00 13.82 ? 189 ASP A N   1 
ATOM   985  C  CA  . ASP A 1 189 ? 15.995  -11.419 20.938  1.00 16.06 ? 189 ASP A CA  1 
ATOM   986  C  C   . ASP A 1 189 ? 15.566  -10.576 22.132  1.00 16.70 ? 189 ASP A C   1 
ATOM   987  O  O   . ASP A 1 189 ? 14.373  -10.401 22.287  1.00 19.40 ? 189 ASP A O   1 
ATOM   988  C  CB  . ASP A 1 189 ? 15.603  -12.864 21.125  1.00 16.78 ? 189 ASP A CB  1 
ATOM   989  C  CG  . ASP A 1 189 ? 15.764  -13.674 19.866  1.00 20.59 ? 189 ASP A CG  1 
ATOM   990  O  OD1 . ASP A 1 189 ? 15.473  -13.151 18.758  1.00 17.38 ? 189 ASP A OD1 1 
ATOM   991  O  OD2 . ASP A 1 189 ? 16.218  -14.801 20.010  1.00 21.06 ? 189 ASP A OD2 1 
ATOM   992  N  N   . ASP A 1 190 ? 16.502  -10.021 22.876  1.00 16.54 ? 190 ASP A N   1 
ATOM   993  C  CA  . ASP A 1 190 ? 16.213  -9.284  24.078  1.00 15.28 ? 190 ASP A CA  1 
ATOM   994  C  C   . ASP A 1 190 ? 16.775  -7.888  23.892  1.00 16.64 ? 190 ASP A C   1 
ATOM   995  O  O   . ASP A 1 190 ? 17.962  -7.690  23.710  1.00 16.34 ? 190 ASP A O   1 
ATOM   996  C  CB  . ASP A 1 190 ? 16.773  -10.057 25.292  1.00 18.70 ? 190 ASP A CB  1 
ATOM   997  C  CG  . ASP A 1 190 ? 16.591  -9.364  26.633  1.00 21.25 ? 190 ASP A CG  1 
ATOM   998  O  OD1 . ASP A 1 190 ? 16.506  -8.120  26.654  1.00 20.22 ? 190 ASP A OD1 1 
ATOM   999  O  OD2 . ASP A 1 190 ? 16.598  -10.043 27.655  1.00 21.96 ? 190 ASP A OD2 1 
ATOM   1000 N  N   . PRO A 1 191 ? 15.951  -6.816  23.926  1.00 17.46 ? 191 PRO A N   1 
ATOM   1001 C  CA  . PRO A 1 191 ? 16.434  -5.453  23.656  1.00 16.13 ? 191 PRO A CA  1 
ATOM   1002 C  C   . PRO A 1 191 ? 17.469  -4.999  24.659  1.00 16.26 ? 191 PRO A C   1 
ATOM   1003 O  O   . PRO A 1 191 ? 18.309  -4.188  24.341  1.00 17.01 ? 191 PRO A O   1 
ATOM   1004 C  CB  . PRO A 1 191 ? 15.126  -4.606  23.672  1.00 17.39 ? 191 PRO A CB  1 
ATOM   1005 C  CG  . PRO A 1 191 ? 14.125  -5.417  24.498  1.00 18.93 ? 191 PRO A CG  1 
ATOM   1006 C  CD  . PRO A 1 191 ? 14.496  -6.882  24.227  1.00 18.56 ? 191 PRO A CD  1 
ATOM   1007 N  N   . GLN A 1 192 ? 17.386  -5.493  25.927  1.00 14.65 ? 192 GLN A N   1 
ATOM   1008 C  CA  . GLN A 1 192 ? 18.306  -5.069  26.958  1.00 16.58 ? 192 GLN A CA  1 
ATOM   1009 C  C   . GLN A 1 192 ? 19.697  -5.642  26.659  1.00 15.81 ? 192 GLN A C   1 
ATOM   1010 O  O   . GLN A 1 192 ? 20.696  -4.979  26.893  1.00 15.00 ? 192 GLN A O   1 
ATOM   1011 C  CB  . GLN A 1 192 ? 17.774  -5.477  28.343  1.00 16.43 ? 192 GLN A CB  1 
ATOM   1012 C  CG  . GLN A 1 192 ? 18.561  -4.868  29.472  1.00 17.37 ? 192 GLN A CG  1 
ATOM   1013 C  CD  . GLN A 1 192 ? 17.669  -4.586  30.686  1.00 19.96 ? 192 GLN A CD  1 
ATOM   1014 O  OE1 . GLN A 1 192 ? 16.457  -4.347  30.521  1.00 22.93 ? 192 GLN A OE1 1 
ATOM   1015 N  NE2 . GLN A 1 192 ? 18.229  -4.722  31.886  1.00 17.66 ? 192 GLN A NE2 1 
ATOM   1016 N  N   . VAL A 1 193 ? 19.731  -6.856  26.098  1.00 17.88 ? 193 VAL A N   1 
ATOM   1017 C  CA  . VAL A 1 193 ? 21.007  -7.469  25.693  1.00 16.60 ? 193 VAL A CA  1 
ATOM   1018 C  C   . VAL A 1 193 ? 21.640  -6.620  24.597  1.00 17.20 ? 193 VAL A C   1 
ATOM   1019 O  O   . VAL A 1 193 ? 22.861  -6.358  24.608  1.00 15.84 ? 193 VAL A O   1 
ATOM   1020 C  CB  . VAL A 1 193 ? 20.794  -8.928  25.265  1.00 17.28 ? 193 VAL A CB  1 
ATOM   1021 C  CG1 . VAL A 1 193 ? 22.023  -9.534  24.587  1.00 21.05 ? 193 VAL A CG1 1 
ATOM   1022 C  CG2 . VAL A 1 193 ? 20.417  -9.757  26.510  1.00 19.95 ? 193 VAL A CG2 1 
ATOM   1023 N  N   . ALA A 1 194 ? 20.799  -6.178  23.641  1.00 15.45 ? 194 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 194 ? 21.314  -5.371  22.541  1.00 16.75 ? 194 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 194 ? 21.817  -4.016  23.006  1.00 13.95 ? 194 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 194 ? 22.907  -3.539  22.607  1.00 14.96 ? 194 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 194 ? 20.300  -5.297  21.423  1.00 16.61 ? 194 ALA A CB  1 
ATOM   1028 N  N   . VAL A 1 195 ? 21.044  -3.319  23.850  1.00 14.50 ? 195 VAL A N   1 
ATOM   1029 C  CA  . VAL A 1 195 ? 21.457  -1.968  24.325  1.00 17.73 ? 195 VAL A CA  1 
ATOM   1030 C  C   . VAL A 1 195 ? 22.749  -2.062  25.128  1.00 13.78 ? 195 VAL A C   1 
ATOM   1031 O  O   . VAL A 1 195 ? 23.685  -1.299  24.950  1.00 14.70 ? 195 VAL A O   1 
ATOM   1032 C  CB  . VAL A 1 195 ? 20.316  -1.317  25.135  1.00 20.73 ? 195 VAL A CB  1 
ATOM   1033 C  CG1 . VAL A 1 195 ? 20.752  -0.053  25.838  1.00 28.10 ? 195 VAL A CG1 1 
ATOM   1034 C  CG2 . VAL A 1 195 ? 19.118  -1.057  24.239  1.00 25.03 ? 195 VAL A CG2 1 
ATOM   1035 N  N   . HIS A 1 196 ? 22.857  -3.123  25.978  1.00 12.96 ? 196 HIS A N   1 
ATOM   1036 C  CA  . HIS A 1 196 ? 23.996  -3.333  26.810  1.00 13.60 ? 196 HIS A CA  1 
ATOM   1037 C  C   . HIS A 1 196 ? 25.260  -3.451  25.969  1.00 14.44 ? 196 HIS A C   1 
ATOM   1038 O  O   . HIS A 1 196 ? 26.276  -2.862  26.292  1.00 15.81 ? 196 HIS A O   1 
ATOM   1039 C  CB  . HIS A 1 196 ? 23.750  -4.598  27.685  1.00 15.39 ? 196 HIS A CB  1 
ATOM   1040 C  CG  . HIS A 1 196 ? 24.976  -5.018  28.448  1.00 16.06 ? 196 HIS A CG  1 
ATOM   1041 N  ND1 . HIS A 1 196 ? 25.791  -6.032  27.990  1.00 16.81 ? 196 HIS A ND1 1 
ATOM   1042 C  CD2 . HIS A 1 196 ? 25.534  -4.557  29.633  1.00 16.24 ? 196 HIS A CD2 1 
ATOM   1043 C  CE1 . HIS A 1 196 ? 26.811  -6.190  28.844  1.00 16.71 ? 196 HIS A CE1 1 
ATOM   1044 N  NE2 . HIS A 1 196 ? 26.687  -5.270  29.867  1.00 18.01 ? 196 HIS A NE2 1 
ATOM   1045 N  N   . ALA A 1 197 ? 25.139  -4.211  24.853  1.00 14.64 ? 197 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 197 ? 26.271  -4.416  23.969  1.00 13.87 ? 197 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 197 ? 26.746  -3.080  23.383  1.00 13.57 ? 197 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 197 ? 27.908  -2.767  23.444  1.00 14.90 ? 197 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 197 ? 25.890  -5.430  22.921  1.00 14.92 ? 197 ALA A CB  1 
ATOM   1050 N  N   . ILE A 1 198 ? 25.823  -2.282  22.819  1.00 14.05 ? 198 ILE A N   1 
ATOM   1051 C  CA  . ILE A 1 198 ? 26.166  -1.013  22.215  1.00 14.26 ? 198 ILE A CA  1 
ATOM   1052 C  C   . ILE A 1 198 ? 26.731  -0.029  23.245  1.00 14.67 ? 198 ILE A C   1 
ATOM   1053 O  O   . ILE A 1 198 ? 27.753  0.588   23.018  1.00 17.93 ? 198 ILE A O   1 
ATOM   1054 C  CB  . ILE A 1 198 ? 24.957  -0.406  21.476  1.00 14.51 ? 198 ILE A CB  1 
ATOM   1055 C  CG1 . ILE A 1 198 ? 24.534  -1.291  20.306  1.00 17.23 ? 198 ILE A CG1 1 
ATOM   1056 C  CG2 . ILE A 1 198 ? 25.332  0.997   20.971  1.00 16.97 ? 198 ILE A CG2 1 
ATOM   1057 C  CD1 . ILE A 1 198 ? 25.539  -1.454  19.197  1.00 17.17 ? 198 ILE A CD1 1 
ATOM   1058 N  N   . ARG A 1 199 ? 26.090  0.041   24.380  1.00 16.10 ? 199 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 199 ? 26.543  0.907   25.457  1.00 14.94 ? 199 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 199 ? 27.941  0.572   25.951  1.00 14.82 ? 199 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 199 ? 28.786  1.464   26.120  1.00 16.04 ? 199 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 199 ? 25.536  0.824   26.573  1.00 16.09 ? 199 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 199 ? 25.896  1.658   27.790  1.00 17.85 ? 199 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 199 ? 25.238  0.970   28.929  1.00 18.62 ? 199 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 199 ? 25.317  1.724   30.177  1.00 14.90 ? 199 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 199 ? 24.344  1.670   31.099  1.00 17.22 ? 199 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 199 ? 23.293  0.905   30.820  1.00 15.74 ? 199 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 199 ? 24.508  2.234   32.290  1.00 15.87 ? 199 ARG A NH2 1 
ATOM   1069 N  N   . ASN A 1 200 ? 28.236  -0.725  26.116  1.00 14.44 ? 200 ASN A N   1 
ATOM   1070 C  CA  . ASN A 1 200 ? 29.570  -1.121  26.529  1.00 16.34 ? 200 ASN A CA  1 
ATOM   1071 C  C   . ASN A 1 200 ? 30.639  -0.894  25.469  1.00 14.32 ? 200 ASN A C   1 
ATOM   1072 O  O   . ASN A 1 200 ? 31.727  -0.444  25.770  1.00 17.30 ? 200 ASN A O   1 
ATOM   1073 C  CB  . ASN A 1 200 ? 29.512  -2.517  27.160  1.00 15.17 ? 200 ASN A CB  1 
ATOM   1074 C  CG  . ASN A 1 200 ? 28.977  -2.442  28.589  1.00 16.02 ? 200 ASN A CG  1 
ATOM   1075 O  OD1 . ASN A 1 200 ? 29.788  -2.283  29.520  1.00 17.54 ? 200 ASN A OD1 1 
ATOM   1076 N  ND2 . ASN A 1 200 ? 27.661  -2.431  28.755  1.00 15.68 ? 200 ASN A ND2 1 
ATOM   1077 N  N   . LEU A 1 201 ? 30.357  -1.148  24.184  1.00 16.87 ? 201 LEU A N   1 
ATOM   1078 C  CA  . LEU A 1 201 ? 31.305  -0.806  23.138  1.00 16.50 ? 201 LEU A CA  1 
ATOM   1079 C  C   . LEU A 1 201 ? 31.580  0.692   23.112  1.00 15.44 ? 201 LEU A C   1 
ATOM   1080 O  O   . LEU A 1 201 ? 32.713  1.113   22.985  1.00 15.52 ? 201 LEU A O   1 
ATOM   1081 C  CB  . LEU A 1 201 ? 30.770  -1.330  21.787  1.00 16.89 ? 201 LEU A CB  1 
ATOM   1082 C  CG  . LEU A 1 201 ? 30.734  -2.871  21.674  1.00 19.20 ? 201 LEU A CG  1 
ATOM   1083 C  CD1 . LEU A 1 201 ? 30.140  -3.322  20.383  1.00 21.08 ? 201 LEU A CD1 1 
ATOM   1084 C  CD2 . LEU A 1 201 ? 32.104  -3.564  21.856  1.00 20.09 ? 201 LEU A CD2 1 
ATOM   1085 N  N   . ALA A 1 202 ? 30.542  1.492   23.152  1.00 17.33 ? 202 ALA A N   1 
ATOM   1086 C  CA  . ALA A 1 202 ? 30.727  2.932   23.137  1.00 19.05 ? 202 ALA A CA  1 
ATOM   1087 C  C   . ALA A 1 202 ? 31.566  3.400   24.317  1.00 17.81 ? 202 ALA A C   1 
ATOM   1088 O  O   . ALA A 1 202 ? 32.465  4.212   24.150  1.00 21.64 ? 202 ALA A O   1 
ATOM   1089 C  CB  . ALA A 1 202 ? 29.407  3.630   23.128  1.00 17.77 ? 202 ALA A CB  1 
ATOM   1090 N  N   . ARG A 1 203 ? 31.337  2.831   25.490  1.00 20.02 ? 203 ARG A N   1 
ATOM   1091 C  CA  . ARG A 1 203 ? 32.130  3.186   26.671  1.00 20.93 ? 203 ARG A CA  1 
ATOM   1092 C  C   . ARG A 1 203 ? 33.608  2.840   26.511  1.00 20.65 ? 203 ARG A C   1 
ATOM   1093 O  O   . ARG A 1 203 ? 34.512  3.632   26.783  1.00 20.21 ? 203 ARG A O   1 
ATOM   1094 C  CB  . ARG A 1 203 ? 31.443  2.475   27.836  1.00 21.15 ? 203 ARG A CB  1 
ATOM   1095 C  CG  . ARG A 1 203 ? 32.206  2.628   29.137  1.00 26.44 ? 203 ARG A CG  1 
ATOM   1096 C  CD  . ARG A 1 203 ? 31.315  2.211   30.267  1.00 26.85 ? 203 ARG A CD  1 
ATOM   1097 N  NE  . ARG A 1 203 ? 31.998  2.524   31.526  1.00 29.78 ? 203 ARG A NE  1 
ATOM   1098 C  CZ  . ARG A 1 203 ? 32.685  1.610   32.228  1.00 31.49 ? 203 ARG A CZ  1 
ATOM   1099 N  NH1 . ARG A 1 203 ? 32.559  0.330   31.931  1.00 27.84 ? 203 ARG A NH1 1 
ATOM   1100 N  NH2 . ARG A 1 203 ? 33.480  1.979   33.217  1.00 33.32 ? 203 ARG A NH2 1 
ATOM   1101 N  N   . ILE A 1 204 ? 33.884  1.604   26.067  1.00 19.44 ? 204 ILE A N   1 
ATOM   1102 C  CA  . ILE A 1 204 ? 35.231  1.167   25.748  1.00 22.67 ? 204 ILE A CA  1 
ATOM   1103 C  C   . ILE A 1 204 ? 35.889  2.152   24.776  1.00 23.37 ? 204 ILE A C   1 
ATOM   1104 O  O   . ILE A 1 204 ? 37.061  2.434   24.892  1.00 21.79 ? 204 ILE A O   1 
ATOM   1105 C  CB  . ILE A 1 204 ? 35.244  -0.302  25.242  1.00 21.55 ? 204 ILE A CB  1 
ATOM   1106 C  CG1 . ILE A 1 204 ? 34.838  -1.263  26.363  1.00 26.37 ? 204 ILE A CG1 1 
ATOM   1107 C  CG2 . ILE A 1 204 ? 36.611  -0.684  24.630  1.00 24.59 ? 204 ILE A CG2 1 
ATOM   1108 C  CD1 . ILE A 1 204 ? 34.549  -2.677  25.917  1.00 24.11 ? 204 ILE A CD1 1 
ATOM   1109 N  N   . GLY A 1 205 ? 35.140  2.669   23.779  1.00 24.06 ? 205 GLY A N   1 
ATOM   1110 C  CA  . GLY A 1 205 ? 35.704  3.520   22.740  1.00 25.34 ? 205 GLY A CA  1 
ATOM   1111 C  C   . GLY A 1 205 ? 35.817  5.016   23.071  1.00 24.02 ? 205 GLY A C   1 
ATOM   1112 O  O   . GLY A 1 205 ? 36.173  5.809   22.207  1.00 22.53 ? 205 GLY A O   1 
ATOM   1113 N  N   . PHE A 1 206 ? 35.424  5.413   24.285  1.00 23.66 ? 206 PHE A N   1 
ATOM   1114 C  CA  . PHE A 1 206 ? 35.428  6.806   24.705  1.00 34.48 ? 206 PHE A CA  1 
ATOM   1115 C  C   . PHE A 1 206 ? 36.807  7.408   24.431  1.00 29.94 ? 206 PHE A C   1 
ATOM   1116 O  O   . PHE A 1 206 ? 37.845  6.782   24.685  1.00 29.12 ? 206 PHE A O   1 
ATOM   1117 C  CB  . PHE A 1 206 ? 35.041  6.905   26.184  1.00 38.80 ? 206 PHE A CB  1 
ATOM   1118 C  CG  . PHE A 1 206 ? 35.096  8.299   26.762  1.00 49.03 ? 206 PHE A CG  1 
ATOM   1119 C  CD1 . PHE A 1 206 ? 34.021  9.175   26.610  1.00 55.76 ? 206 PHE A CD1 1 
ATOM   1120 C  CD2 . PHE A 1 206 ? 36.237  8.744   27.436  1.00 56.83 ? 206 PHE A CD2 1 
ATOM   1121 C  CE1 . PHE A 1 206 ? 34.072  10.459  27.148  1.00 63.86 ? 206 PHE A CE1 1 
ATOM   1122 C  CE2 . PHE A 1 206 ? 36.294  10.035  27.948  1.00 60.87 ? 206 PHE A CE2 1 
ATOM   1123 C  CZ  . PHE A 1 206 ? 35.211  10.890  27.808  1.00 58.97 ? 206 PHE A CZ  1 
ATOM   1124 N  N   . GLY A 1 207 ? 36.819  8.592   23.810  1.00 29.36 ? 207 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 207 ? 38.065  9.227   23.395  1.00 29.99 ? 207 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 207 ? 38.540  8.871   21.979  1.00 29.97 ? 207 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 207 ? 39.356  9.588   21.423  1.00 30.24 ? 207 GLY A O   1 
ATOM   1128 N  N   . LYS A 1 208 ? 38.063  7.760   21.375  1.00 23.22 ? 208 LYS A N   1 
ATOM   1129 C  CA  . LYS A 1 208 ? 38.546  7.302   20.075  1.00 21.24 ? 208 LYS A CA  1 
ATOM   1130 C  C   . LYS A 1 208 ? 37.433  7.294   19.035  1.00 19.76 ? 208 LYS A C   1 
ATOM   1131 O  O   . LYS A 1 208 ? 37.694  7.359   17.831  1.00 23.81 ? 208 LYS A O   1 
ATOM   1132 C  CB  . LYS A 1 208 ? 39.190  5.922   20.180  1.00 29.58 ? 208 LYS A CB  1 
ATOM   1133 C  CG  . LYS A 1 208 ? 40.338  5.807   21.186  1.00 31.24 ? 208 LYS A CG  1 
ATOM   1134 C  CD  . LYS A 1 208 ? 40.899  4.425   21.205  1.00 34.31 ? 208 LYS A CD  1 
ATOM   1135 C  CE  . LYS A 1 208 ? 41.902  4.150   22.328  1.00 37.03 ? 208 LYS A CE  1 
ATOM   1136 N  NZ  . LYS A 1 208 ? 42.741  2.959   22.010  1.00 29.86 ? 208 LYS A NZ  1 
ATOM   1137 N  N   . VAL A 1 209 ? 36.193  7.094   19.510  1.00 20.33 ? 209 VAL A N   1 
ATOM   1138 C  CA  . VAL A 1 209 ? 34.990  7.084   18.655  1.00 22.35 ? 209 VAL A CA  1 
ATOM   1139 C  C   . VAL A 1 209 ? 33.869  7.770   19.422  1.00 20.34 ? 209 VAL A C   1 
ATOM   1140 O  O   . VAL A 1 209 ? 33.849  7.754   20.658  1.00 23.14 ? 209 VAL A O   1 
ATOM   1141 C  CB  . VAL A 1 209 ? 34.525  5.673   18.206  1.00 20.76 ? 209 VAL A CB  1 
ATOM   1142 C  CG1 . VAL A 1 209 ? 35.540  4.997   17.308  1.00 25.29 ? 209 VAL A CG1 1 
ATOM   1143 C  CG2 . VAL A 1 209 ? 34.143  4.777   19.343  1.00 19.81 ? 209 VAL A CG2 1 
ATOM   1144 N  N   . VAL A 1 210 ? 32.903  8.340   18.689  1.00 20.80 ? 210 VAL A N   1 
ATOM   1145 C  CA  . VAL A 1 210 ? 31.699  8.906   19.257  1.00 21.01 ? 210 VAL A CA  1 
ATOM   1146 C  C   . VAL A 1 210 ? 30.520  8.310   18.508  1.00 22.68 ? 210 VAL A C   1 
ATOM   1147 O  O   . VAL A 1 210 ? 30.649  8.047   17.337  1.00 21.52 ? 210 VAL A O   1 
ATOM   1148 C  CB  . VAL A 1 210 ? 31.623  10.450  19.150  1.00 26.43 ? 210 VAL A CB  1 
ATOM   1149 C  CG1 . VAL A 1 210 ? 32.573  11.128  20.123  1.00 36.44 ? 210 VAL A CG1 1 
ATOM   1150 C  CG2 . VAL A 1 210 ? 31.888  10.934  17.724  1.00 25.07 ? 210 VAL A CG2 1 
ATOM   1151 N  N   . VAL A 1 211 ? 29.365  8.188   19.163  1.00 22.67 ? 211 VAL A N   1 
ATOM   1152 C  CA  . VAL A 1 211 ? 28.186  7.805   18.424  1.00 22.10 ? 211 VAL A CA  1 
ATOM   1153 C  C   . VAL A 1 211 ? 27.687  8.991   17.599  1.00 23.81 ? 211 VAL A C   1 
ATOM   1154 O  O   . VAL A 1 211 ? 27.428  10.063  18.130  1.00 24.11 ? 211 VAL A O   1 
ATOM   1155 C  CB  . VAL A 1 211 ? 27.065  7.230   19.293  1.00 22.03 ? 211 VAL A CB  1 
ATOM   1156 C  CG1 . VAL A 1 211 ? 25.928  6.746   18.403  1.00 22.04 ? 211 VAL A CG1 1 
ATOM   1157 C  CG2 . VAL A 1 211 ? 27.596  6.111   20.182  1.00 27.06 ? 211 VAL A CG2 1 
ATOM   1158 N  N   . ARG A 1 212 ? 27.598  8.765   16.285  1.00 19.99 ? 212 ARG A N   1 
ATOM   1159 C  CA  . ARG A 1 212 ? 27.034  9.733   15.356  1.00 18.46 ? 212 ARG A CA  1 
ATOM   1160 C  C   . ARG A 1 212 ? 25.494  9.698   15.363  1.00 18.70 ? 212 ARG A C   1 
ATOM   1161 O  O   . ARG A 1 212 ? 24.816  10.684  15.601  1.00 20.80 ? 212 ARG A O   1 
ATOM   1162 C  CB  . ARG A 1 212 ? 27.563  9.459   13.958  1.00 19.61 ? 212 ARG A CB  1 
ATOM   1163 C  CG  . ARG A 1 212 ? 27.120  10.473  12.923  1.00 20.36 ? 212 ARG A CG  1 
ATOM   1164 C  CD  . ARG A 1 212 ? 27.512  10.101  11.535  1.00 21.23 ? 212 ARG A CD  1 
ATOM   1165 N  NE  . ARG A 1 212 ? 27.050  11.086  10.585  1.00 25.75 ? 212 ARG A NE  1 
ATOM   1166 C  CZ  . ARG A 1 212 ? 27.560  12.324  10.432  1.00 34.61 ? 212 ARG A CZ  1 
ATOM   1167 N  NH1 . ARG A 1 212 ? 28.737  12.668  10.975  1.00 28.63 ? 212 ARG A NH1 1 
ATOM   1168 N  NH2 . ARG A 1 212 ? 26.922  13.203  9.671   1.00 31.18 ? 212 ARG A NH2 1 
ATOM   1169 N  N   . TRP A 1 213 ? 24.910  8.510   15.186  1.00 18.60 ? 213 TRP A N   1 
ATOM   1170 C  CA  . TRP A 1 213 ? 23.473  8.335   15.257  1.00 17.48 ? 213 TRP A CA  1 
ATOM   1171 C  C   . TRP A 1 213 ? 23.175  6.883   15.582  1.00 17.40 ? 213 TRP A C   1 
ATOM   1172 O  O   . TRP A 1 213 ? 24.031  6.062   15.462  1.00 17.21 ? 213 TRP A O   1 
ATOM   1173 C  CB  . TRP A 1 213 ? 22.800  8.720   13.933  1.00 17.94 ? 213 TRP A CB  1 
ATOM   1174 C  CG  . TRP A 1 213 ? 23.238  7.965   12.697  1.00 17.24 ? 213 TRP A CG  1 
ATOM   1175 C  CD1 . TRP A 1 213 ? 24.112  8.404   11.756  1.00 17.08 ? 213 TRP A CD1 1 
ATOM   1176 C  CD2 . TRP A 1 213 ? 22.691  6.747   12.160  1.00 19.44 ? 213 TRP A CD2 1 
ATOM   1177 N  NE1 . TRP A 1 213 ? 24.298  7.493   10.775  1.00 22.09 ? 213 TRP A NE1 1 
ATOM   1178 C  CE2 . TRP A 1 213 ? 23.403  6.472   10.972  1.00 20.21 ? 213 TRP A CE2 1 
ATOM   1179 C  CE3 . TRP A 1 213 ? 21.787  5.786   12.642  1.00 19.63 ? 213 TRP A CE3 1 
ATOM   1180 C  CZ2 . TRP A 1 213 ? 23.160  5.334   10.204  1.00 21.81 ? 213 TRP A CZ2 1 
ATOM   1181 C  CZ3 . TRP A 1 213 ? 21.527  4.677   11.860  1.00 23.73 ? 213 TRP A CZ3 1 
ATOM   1182 C  CH2 . TRP A 1 213 ? 22.179  4.478   10.637  1.00 23.35 ? 213 TRP A CH2 1 
ATOM   1183 N  N   . SER A 1 214 ? 21.974  6.599   16.092  1.00 15.31 ? 214 SER A N   1 
ATOM   1184 C  CA  . SER A 1 214 ? 21.621  5.231   16.376  1.00 18.21 ? 214 SER A CA  1 
ATOM   1185 C  C   . SER A 1 214 ? 20.168  5.040   15.983  1.00 19.79 ? 214 SER A C   1 
ATOM   1186 O  O   . SER A 1 214 ? 19.449  6.018   15.770  1.00 19.62 ? 214 SER A O   1 
ATOM   1187 C  CB  . SER A 1 214 ? 21.906  4.884   17.789  1.00 23.83 ? 214 SER A CB  1 
ATOM   1188 O  OG  . SER A 1 214 ? 21.052  5.585   18.666  1.00 25.68 ? 214 SER A OG  1 
ATOM   1189 N  N   . GLN A 1 215 ? 19.775  3.794   15.839  1.00 14.77 ? 215 GLN A N   1 
ATOM   1190 C  CA  . GLN A 1 215 ? 18.440  3.421   15.485  1.00 16.45 ? 215 GLN A CA  1 
ATOM   1191 C  C   . GLN A 1 215 ? 18.071  2.105   16.176  1.00 16.22 ? 215 GLN A C   1 
ATOM   1192 O  O   . GLN A 1 215 ? 18.800  1.126   16.029  1.00 16.88 ? 215 GLN A O   1 
ATOM   1193 C  CB  . GLN A 1 215 ? 18.323  3.241   13.965  1.00 18.88 ? 215 GLN A CB  1 
ATOM   1194 C  CG  . GLN A 1 215 ? 16.889  2.886   13.579  1.00 18.22 ? 215 GLN A CG  1 
ATOM   1195 C  CD  . GLN A 1 215 ? 15.886  3.999   13.785  1.00 18.99 ? 215 GLN A CD  1 
ATOM   1196 O  OE1 . GLN A 1 215 ? 16.131  5.081   13.256  1.00 23.15 ? 215 GLN A OE1 1 
ATOM   1197 N  NE2 . GLN A 1 215 ? 14.878  3.788   14.647  1.00 17.21 ? 215 GLN A NE2 1 
ATOM   1198 N  N   . LEU A 1 216 ? 16.987  2.134   16.951  1.00 15.48 ? 216 LEU A N   1 
ATOM   1199 C  CA  . LEU A 1 216 ? 16.430  0.932   17.534  1.00 17.73 ? 216 LEU A CA  1 
ATOM   1200 C  C   . LEU A 1 216 ? 15.314  0.426   16.640  1.00 19.66 ? 216 LEU A C   1 
ATOM   1201 O  O   . LEU A 1 216 ? 14.542  1.248   16.127  1.00 18.09 ? 216 LEU A O   1 
ATOM   1202 C  CB  . LEU A 1 216 ? 15.957  1.194   18.940  1.00 20.27 ? 216 LEU A CB  1 
ATOM   1203 C  CG  . LEU A 1 216 ? 17.185  1.205   19.850  1.00 23.22 ? 216 LEU A CG  1 
ATOM   1204 C  CD1 . LEU A 1 216 ? 17.877  2.568   19.919  1.00 24.90 ? 216 LEU A CD1 1 
ATOM   1205 C  CD2 . LEU A 1 216 ? 16.789  0.689   21.198  1.00 31.84 ? 216 LEU A CD2 1 
ATOM   1206 N  N   . GLY A 1 217 ? 15.284  -0.903  16.468  1.00 15.69 ? 217 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 217 ? 14.249  -1.588  15.723  1.00 14.87 ? 217 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 217 ? 13.477  -2.488  16.676  1.00 14.54 ? 217 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 217 ? 14.088  -3.373  17.297  1.00 14.94 ? 217 GLY A O   1 
ATOM   1210 N  N   . PHE A 1 218 ? 12.171  -2.240  16.855  1.00 13.08 ? 218 PHE A N   1 
ATOM   1211 C  CA  . PHE A 1 218 ? 11.423  -2.953  17.898  1.00 14.77 ? 218 PHE A CA  1 
ATOM   1212 C  C   . PHE A 1 218 ? 11.048  -4.343  17.460  1.00 15.16 ? 218 PHE A C   1 
ATOM   1213 O  O   . PHE A 1 218 ? 10.691  -5.167  18.296  1.00 18.81 ? 218 PHE A O   1 
ATOM   1214 C  CB  . PHE A 1 218 ? 10.215  -2.195  18.429  1.00 14.13 ? 218 PHE A CB  1 
ATOM   1215 C  CG  . PHE A 1 218 ? 9.099   -1.977  17.428  1.00 13.56 ? 218 PHE A CG  1 
ATOM   1216 C  CD1 . PHE A 1 218 ? 8.233   -3.000  17.158  1.00 13.44 ? 218 PHE A CD1 1 
ATOM   1217 C  CD2 . PHE A 1 218 ? 8.914   -0.777  16.786  1.00 16.31 ? 218 PHE A CD2 1 
ATOM   1218 C  CE1 . PHE A 1 218 ? 7.256   -2.880  16.195  1.00 15.36 ? 218 PHE A CE1 1 
ATOM   1219 C  CE2 . PHE A 1 218 ? 7.876   -0.598  15.886  1.00 14.33 ? 218 PHE A CE2 1 
ATOM   1220 C  CZ  . PHE A 1 218 ? 7.052   -1.647  15.585  1.00 15.11 ? 218 PHE A CZ  1 
ATOM   1221 N  N   . GLY A 1 219 ? 11.010  -4.558  16.160  1.00 13.03 ? 219 GLY A N   1 
ATOM   1222 C  CA  . GLY A 1 219 ? 10.470  -5.803  15.617  1.00 15.10 ? 219 GLY A CA  1 
ATOM   1223 C  C   . GLY A 1 219 ? 11.045  -6.010  14.218  1.00 13.21 ? 219 GLY A C   1 
ATOM   1224 O  O   . GLY A 1 219 ? 11.291  -5.053  13.515  1.00 14.22 ? 219 GLY A O   1 
ATOM   1225 N  N   . LYS A 1 220 ? 11.325  -7.253  13.865  1.00 14.23 ? 220 LYS A N   1 
ATOM   1226 C  CA  . LYS A 1 220 ? 11.914  -7.541  12.554  1.00 13.34 ? 220 LYS A CA  1 
ATOM   1227 C  C   . LYS A 1 220 ? 10.866  -7.458  11.449  1.00 12.81 ? 220 LYS A C   1 
ATOM   1228 O  O   . LYS A 1 220 ? 9.662   -7.671  11.662  1.00 14.01 ? 220 LYS A O   1 
ATOM   1229 C  CB  . LYS A 1 220 ? 12.576  -8.922  12.541  1.00 14.70 ? 220 LYS A CB  1 
ATOM   1230 C  CG  . LYS A 1 220 ? 11.600  -10.067 12.712  1.00 16.65 ? 220 LYS A CG  1 
ATOM   1231 C  CD  . LYS A 1 220 ? 12.251  -11.349 13.114  1.00 21.44 ? 220 LYS A CD  1 
ATOM   1232 C  CE  . LYS A 1 220 ? 11.218  -12.402 13.468  1.00 24.84 ? 220 LYS A CE  1 
ATOM   1233 N  NZ  . LYS A 1 220 ? 11.869  -13.737 13.483  1.00 25.43 ? 220 LYS A NZ  1 
ATOM   1234 N  N   A THR A 1 221 ? 11.348  -7.079  10.252  0.70 11.42 ? 221 THR A N   1 
ATOM   1235 N  N   B THR A 1 221 ? 11.359  -7.178  10.238  0.30 11.99 ? 221 THR A N   1 
ATOM   1236 C  CA  A THR A 1 221 ? 10.566  -7.075  9.027   0.70 12.56 ? 221 THR A CA  1 
ATOM   1237 C  CA  B THR A 1 221 ? 10.509  -7.137  9.064   0.30 12.10 ? 221 THR A CA  1 
ATOM   1238 C  C   A THR A 1 221 ? 11.326  -7.800  7.924   0.70 10.95 ? 221 THR A C   1 
ATOM   1239 C  C   B THR A 1 221 ? 11.157  -7.902  7.912   0.30 11.35 ? 221 THR A C   1 
ATOM   1240 O  O   A THR A 1 221 ? 11.415  -7.302  6.834   0.70 11.80 ? 221 THR A O   1 
ATOM   1241 O  O   B THR A 1 221 ? 10.871  -7.624  6.762   0.30 11.13 ? 221 THR A O   1 
ATOM   1242 C  CB  A THR A 1 221 ? 10.293  -5.655  8.515   0.70 13.05 ? 221 THR A CB  1 
ATOM   1243 C  CB  B THR A 1 221 ? 10.189  -5.689  8.683   0.30 11.95 ? 221 THR A CB  1 
ATOM   1244 O  OG1 A THR A 1 221 ? 11.490  -4.899  8.408   0.70 13.58 ? 221 THR A OG1 1 
ATOM   1245 O  OG1 B THR A 1 221 ? 8.901   -5.865  8.085   0.30 12.45 ? 221 THR A OG1 1 
ATOM   1246 C  CG2 A THR A 1 221 ? 9.316   -4.923  9.380   0.70 15.29 ? 221 THR A CG2 1 
ATOM   1247 C  CG2 B THR A 1 221 ? 11.228  -5.053  7.782   0.30 11.66 ? 221 THR A CG2 1 
ATOM   1248 N  N   . SER A 1 222 ? 11.957  -8.919  8.240   1.00 11.97 ? 222 SER A N   1 
ATOM   1249 C  CA  . SER A 1 222 ? 12.792  -9.632  7.287   1.00 11.13 ? 222 SER A CA  1 
ATOM   1250 C  C   . SER A 1 222 ? 12.905  -11.061 7.792   1.00 12.06 ? 222 SER A C   1 
ATOM   1251 O  O   . SER A 1 222 ? 12.571  -11.353 8.911   1.00 12.08 ? 222 SER A O   1 
ATOM   1252 C  CB  . SER A 1 222 ? 14.153  -9.009  7.251   1.00 14.25 ? 222 SER A CB  1 
ATOM   1253 O  OG  . SER A 1 222 ? 14.678  -8.820  8.593   1.00 12.25 ? 222 SER A OG  1 
ATOM   1254 N  N   . SER A 1 223 ? 13.347  -11.930 6.886   1.00 14.59 ? 223 SER A N   1 
ATOM   1255 C  CA  . SER A 1 223 ? 13.509  -13.350 7.154   1.00 15.14 ? 223 SER A CA  1 
ATOM   1256 C  C   . SER A 1 223 ? 14.691  -13.914 6.354   1.00 14.73 ? 223 SER A C   1 
ATOM   1257 O  O   . SER A 1 223 ? 14.783  -13.683 5.151   1.00 13.87 ? 223 SER A O   1 
ATOM   1258 C  CB  . SER A 1 223 ? 12.259  -14.099 6.816   1.00 16.32 ? 223 SER A CB  1 
ATOM   1259 O  OG  . SER A 1 223 ? 12.472  -15.513 6.931   1.00 15.81 ? 223 SER A OG  1 
ATOM   1260 N  N   . THR A 1 224 ? 15.515  -14.732 7.009   1.00 13.02 ? 224 THR A N   1 
ATOM   1261 C  CA  . THR A 1 224 ? 16.531  -15.583 6.372   1.00 14.78 ? 224 THR A CA  1 
ATOM   1262 C  C   . THR A 1 224 ? 16.183  -17.052 6.651   1.00 16.25 ? 224 THR A C   1 
ATOM   1263 O  O   . THR A 1 224 ? 17.037  -17.905 6.504   1.00 15.07 ? 224 THR A O   1 
ATOM   1264 C  CB  . THR A 1 224 ? 17.933  -15.238 6.876   1.00 13.79 ? 224 THR A CB  1 
ATOM   1265 O  OG1 . THR A 1 224 ? 17.913  -15.378 8.300   1.00 13.25 ? 224 THR A OG1 1 
ATOM   1266 C  CG2 . THR A 1 224 ? 18.318  -13.817 6.501   1.00 14.16 ? 224 THR A CG2 1 
ATOM   1267 N  N   . THR A 1 225 ? 14.936  -17.295 7.078   1.00 14.44 ? 225 THR A N   1 
ATOM   1268 C  CA  . THR A 1 225 ? 14.494  -18.621 7.515   1.00 17.23 ? 225 THR A CA  1 
ATOM   1269 C  C   . THR A 1 225 ? 13.105  -18.824 6.901   1.00 17.22 ? 225 THR A C   1 
ATOM   1270 O  O   . THR A 1 225 ? 12.102  -18.590 7.542   1.00 17.20 ? 225 THR A O   1 
ATOM   1271 C  CB  . THR A 1 225 ? 14.472  -18.744 9.049   1.00 16.97 ? 225 THR A CB  1 
ATOM   1272 O  OG1 . THR A 1 225 ? 13.660  -17.691 9.618   1.00 18.02 ? 225 THR A OG1 1 
ATOM   1273 C  CG2 . THR A 1 225 ? 15.856  -18.739 9.660   1.00 18.74 ? 225 THR A CG2 1 
ATOM   1274 N  N   . PRO A 1 226 ? 13.002  -19.331 5.657   1.00 20.67 ? 226 PRO A N   1 
ATOM   1275 C  CA  . PRO A 1 226 ? 11.731  -19.514 4.982   1.00 22.68 ? 226 PRO A CA  1 
ATOM   1276 C  C   . PRO A 1 226 ? 10.834  -20.598 5.583   1.00 22.58 ? 226 PRO A C   1 
ATOM   1277 O  O   . PRO A 1 226 ? 9.627   -20.597 5.301   1.00 26.28 ? 226 PRO A O   1 
ATOM   1278 C  CB  . PRO A 1 226 ? 12.120  -19.923 3.547   1.00 22.09 ? 226 PRO A CB  1 
ATOM   1279 C  CG  . PRO A 1 226 ? 13.479  -20.498 3.694   1.00 25.64 ? 226 PRO A CG  1 
ATOM   1280 C  CD  . PRO A 1 226 ? 14.134  -19.697 4.786   1.00 20.89 ? 226 PRO A CD  1 
ATOM   1281 N  N   . ASP A 1 227 ? 11.413  -21.405 6.464   1.00 25.35 ? 227 ASP A N   1 
ATOM   1282 C  CA  . ASP A 1 227 ? 10.710  -22.449 7.207   1.00 27.63 ? 227 ASP A CA  1 
ATOM   1283 C  C   . ASP A 1 227 ? 9.936   -21.836 8.365   1.00 27.95 ? 227 ASP A C   1 
ATOM   1284 O  O   . ASP A 1 227 ? 9.101   -22.529 8.916   1.00 25.82 ? 227 ASP A O   1 
ATOM   1285 C  CB  . ASP A 1 227 ? 11.642  -23.560 7.753   1.00 25.90 ? 227 ASP A CB  1 
ATOM   1286 C  CG  . ASP A 1 227 ? 12.879  -23.058 8.527   1.00 38.56 ? 227 ASP A CG  1 
ATOM   1287 O  OD1 . ASP A 1 227 ? 13.661  -22.209 7.957   1.00 36.68 ? 227 ASP A OD1 1 
ATOM   1288 O  OD2 . ASP A 1 227 ? 13.118  -23.549 9.675   1.00 50.21 ? 227 ASP A OD2 1 
ATOM   1289 N  N   . LYS A 1 228 ? 10.199  -20.568 8.766   1.00 22.89 ? 228 LYS A N   1 
ATOM   1290 C  CA  . LYS A 1 228 ? 9.467   -19.980 9.873   1.00 20.35 ? 228 LYS A CA  1 
ATOM   1291 C  C   . LYS A 1 228 ? 8.509   -18.926 9.315   1.00 20.33 ? 228 LYS A C   1 
ATOM   1292 O  O   . LYS A 1 228 ? 8.601   -18.535 8.143   1.00 17.72 ? 228 LYS A O   1 
ATOM   1293 C  CB  . LYS A 1 228 ? 10.418  -19.362 10.903  1.00 23.58 ? 228 LYS A CB  1 
ATOM   1294 C  CG  . LYS A 1 228 ? 11.577  -20.223 11.415  1.00 31.26 ? 228 LYS A CG  1 
ATOM   1295 C  CD  . LYS A 1 228 ? 11.182  -21.446 12.144  1.00 33.37 ? 228 LYS A CD  1 
ATOM   1296 N  N   . GLN A 1 229 ? 7.586   -18.464 10.177  1.00 18.79 ? 229 GLN A N   1 
ATOM   1297 C  CA  . GLN A 1 229 ? 6.583   -17.467 9.786   1.00 17.38 ? 229 GLN A CA  1 
ATOM   1298 C  C   . GLN A 1 229 ? 7.300   -16.170 9.331   1.00 14.30 ? 229 GLN A C   1 
ATOM   1299 O  O   . GLN A 1 229 ? 8.213   -15.661 9.978   1.00 13.72 ? 229 GLN A O   1 
ATOM   1300 C  CB  . GLN A 1 229 ? 5.642   -17.235 10.981  1.00 19.69 ? 229 GLN A CB  1 
ATOM   1301 C  CG  . GLN A 1 229 ? 4.556   -16.163 10.792  1.00 30.44 ? 229 GLN A CG  1 
ATOM   1302 C  CD  . GLN A 1 229 ? 3.596   -15.882 11.957  1.00 40.33 ? 229 GLN A CD  1 
ATOM   1303 O  OE1 . GLN A 1 229 ? 3.731   -14.917 12.714  1.00 39.96 ? 229 GLN A OE1 1 
ATOM   1304 N  NE2 . GLN A 1 229 ? 2.536   -16.666 12.069  1.00 45.15 ? 229 GLN A NE2 1 
ATOM   1305 N  N   . THR A 1 230 ? 6.827   -15.617 8.221   1.00 13.80 ? 230 THR A N   1 
ATOM   1306 C  CA  . THR A 1 230 ? 7.328   -14.342 7.723   1.00 12.25 ? 230 THR A CA  1 
ATOM   1307 C  C   . THR A 1 230 ? 6.709   -13.209 8.539   1.00 10.96 ? 230 THR A C   1 
ATOM   1308 O  O   . THR A 1 230 ? 5.496   -13.198 8.715   1.00 11.52 ? 230 THR A O   1 
ATOM   1309 C  CB  . THR A 1 230 ? 6.945   -14.224 6.234   1.00 12.79 ? 230 THR A CB  1 
ATOM   1310 O  OG1 . THR A 1 230 ? 7.472   -15.394 5.602   1.00 16.21 ? 230 THR A OG1 1 
ATOM   1311 C  CG2 . THR A 1 230 ? 7.542   -12.983 5.598   1.00 12.58 ? 230 THR A CG2 1 
ATOM   1312 N  N   . PRO A 1 231 ? 7.494   -12.265 9.064   1.00 11.33 ? 231 PRO A N   1 
ATOM   1313 C  CA  . PRO A 1 231 ? 6.945   -11.180 9.868   1.00 11.11 ? 231 PRO A CA  1 
ATOM   1314 C  C   . PRO A 1 231 ? 6.330   -10.134 9.002   1.00 12.75 ? 231 PRO A C   1 
ATOM   1315 O  O   . PRO A 1 231 ? 6.584   -10.099 7.801   1.00 14.88 ? 231 PRO A O   1 
ATOM   1316 C  CB  . PRO A 1 231 ? 8.157   -10.586 10.576  1.00 11.78 ? 231 PRO A CB  1 
ATOM   1317 C  CG  . PRO A 1 231 ? 9.256   -10.853 9.594   1.00 12.56 ? 231 PRO A CG  1 
ATOM   1318 C  CD  . PRO A 1 231 ? 8.955   -12.197 8.949   1.00 10.90 ? 231 PRO A CD  1 
ATOM   1319 N  N   . ARG A 1 232 ? 5.437   -9.361  9.612   1.00 12.04 ? 232 ARG A N   1 
ATOM   1320 C  CA  . ARG A 1 232 ? 4.798   -8.235  8.923   1.00 11.91 ? 232 ARG A CA  1 
ATOM   1321 C  C   . ARG A 1 232 ? 5.431   -6.909  9.265   1.00 12.00 ? 232 ARG A C   1 
ATOM   1322 O  O   . ARG A 1 232 ? 5.806   -6.666  10.401  1.00 11.51 ? 232 ARG A O   1 
ATOM   1323 C  CB  . ARG A 1 232 ? 3.315   -8.226  9.232   1.00 12.65 ? 232 ARG A CB  1 
ATOM   1324 C  CG  . ARG A 1 232 ? 2.599   -9.455  8.663   1.00 13.90 ? 232 ARG A CG  1 
ATOM   1325 C  CD  . ARG A 1 232 ? 1.156   -9.443  8.997   1.00 14.54 ? 232 ARG A CD  1 
ATOM   1326 N  NE  . ARG A 1 232 ? 0.552   -10.674 8.574   1.00 15.04 ? 232 ARG A NE  1 
ATOM   1327 C  CZ  . ARG A 1 232 ? -0.116  -10.865 7.464   1.00 14.72 ? 232 ARG A CZ  1 
ATOM   1328 N  NH1 . ARG A 1 232 ? -0.305  -9.871  6.627   1.00 14.73 ? 232 ARG A NH1 1 
ATOM   1329 N  NH2 . ARG A 1 232 ? -0.614  -12.085 7.215   1.00 15.56 ? 232 ARG A NH2 1 
ATOM   1330 N  N   . ASN A 1 233 ? 5.470   -5.991  8.273   1.00 10.32 ? 233 ASN A N   1 
ATOM   1331 C  CA  . ASN A 1 233 ? 5.847   -4.614  8.504   1.00 12.11 ? 233 ASN A CA  1 
ATOM   1332 C  C   . ASN A 1 233 ? 4.618   -3.831  9.013   1.00 11.39 ? 233 ASN A C   1 
ATOM   1333 O  O   . ASN A 1 233 ? 3.528   -4.386  9.134   1.00 11.12 ? 233 ASN A O   1 
ATOM   1334 C  CB  . ASN A 1 233 ? 6.538   -4.037  7.255   1.00 12.70 ? 233 ASN A CB  1 
ATOM   1335 C  CG  . ASN A 1 233 ? 5.665   -4.068  6.035   1.00 15.25 ? 233 ASN A CG  1 
ATOM   1336 O  OD1 . ASN A 1 233 ? 4.469   -3.786  6.156   1.00 14.65 ? 233 ASN A OD1 1 
ATOM   1337 N  ND2 . ASN A 1 233 ? 6.209   -4.504  4.899   1.00 14.66 ? 233 ASN A ND2 1 
ATOM   1338 N  N   . LEU A 1 234 ? 4.781   -2.512  9.285   1.00 11.06 ? 234 LEU A N   1 
ATOM   1339 C  CA  . LEU A 1 234 ? 3.699   -1.739  9.859   1.00 12.41 ? 234 LEU A CA  1 
ATOM   1340 C  C   . LEU A 1 234 ? 2.636   -1.359  8.822   1.00 12.88 ? 234 LEU A C   1 
ATOM   1341 O  O   . LEU A 1 234 ? 1.613   -0.795  9.197   1.00 16.99 ? 234 LEU A O   1 
ATOM   1342 C  CB  . LEU A 1 234 ? 4.283   -0.507  10.527  1.00 12.97 ? 234 LEU A CB  1 
ATOM   1343 C  CG  . LEU A 1 234 ? 5.020   -0.851  11.837  1.00 17.72 ? 234 LEU A CG  1 
ATOM   1344 C  CD1 . LEU A 1 234 ? 5.615   0.412   12.477  1.00 15.85 ? 234 LEU A CD1 1 
ATOM   1345 C  CD2 . LEU A 1 234 ? 4.089   -1.539  12.800  1.00 20.00 ? 234 LEU A CD2 1 
ATOM   1346 N  N   . LEU A 1 235 ? 2.890   -1.661  7.563   1.00 12.55 ? 235 LEU A N   1 
ATOM   1347 C  CA  . LEU A 1 235 ? 1.816   -1.554  6.591   1.00 13.25 ? 235 LEU A CA  1 
ATOM   1348 C  C   . LEU A 1 235 ? 0.927   -2.786  6.581   1.00 13.79 ? 235 LEU A C   1 
ATOM   1349 O  O   . LEU A 1 235 ? -0.077  -2.840  5.866   1.00 12.59 ? 235 LEU A O   1 
ATOM   1350 C  CB  . LEU A 1 235 ? 2.399   -1.316  5.218   1.00 12.71 ? 235 LEU A CB  1 
ATOM   1351 C  CG  . LEU A 1 235 ? 3.268   -0.079  4.995   1.00 15.92 ? 235 LEU A CG  1 
ATOM   1352 C  CD1 . LEU A 1 235 ? 3.573   0.129   3.511   1.00 16.29 ? 235 LEU A CD1 1 
ATOM   1353 C  CD2 . LEU A 1 235 ? 2.558   1.158   5.540   1.00 15.49 ? 235 LEU A CD2 1 
ATOM   1354 N  N   . GLY A 1 236 ? 1.303   -3.811  7.350   1.00 12.27 ? 236 GLY A N   1 
ATOM   1355 C  CA  . GLY A 1 236 ? 0.475   -4.971  7.541   1.00 11.99 ? 236 GLY A CA  1 
ATOM   1356 C  C   . GLY A 1 236 ? 0.741   -6.116  6.579   1.00 11.03 ? 236 GLY A C   1 
ATOM   1357 O  O   . GLY A 1 236 ? -0.042  -7.081  6.590   1.00 14.78 ? 236 GLY A O   1 
ATOM   1358 N  N   . PHE A 1 237 ? 1.785   -5.971  5.776   1.00 10.60 ? 237 PHE A N   1 
ATOM   1359 C  CA  . PHE A 1 237 ? 2.171   -6.973  4.774   1.00 11.61 ? 237 PHE A CA  1 
ATOM   1360 C  C   . PHE A 1 237 ? 3.359   -7.767  5.278   1.00 11.59 ? 237 PHE A C   1 
ATOM   1361 O  O   . PHE A 1 237 ? 4.262   -7.240  5.922   1.00 12.33 ? 237 PHE A O   1 
ATOM   1362 C  CB  . PHE A 1 237 ? 2.497   -6.405  3.388   1.00 11.18 ? 237 PHE A CB  1 
ATOM   1363 C  CG  . PHE A 1 237 ? 1.295   -6.057  2.559   1.00 10.39 ? 237 PHE A CG  1 
ATOM   1364 C  CD1 . PHE A 1 237 ? 0.537   -4.907  2.827   1.00 10.67 ? 237 PHE A CD1 1 
ATOM   1365 C  CD2 . PHE A 1 237 ? 0.904   -6.846  1.462   1.00 11.89 ? 237 PHE A CD2 1 
ATOM   1366 C  CE1 . PHE A 1 237 ? -0.625  -4.612  2.134   1.00 12.45 ? 237 PHE A CE1 1 
ATOM   1367 C  CE2 . PHE A 1 237 ? -0.268  -6.525  0.780   1.00 12.22 ? 237 PHE A CE2 1 
ATOM   1368 C  CZ  . PHE A 1 237 ? -0.997  -5.409  1.075   1.00 11.35 ? 237 PHE A CZ  1 
ATOM   1369 N  N   . LYS A 1 238 ? 3.315   -9.094  4.983   1.00 11.36 ? 238 LYS A N   1 
ATOM   1370 C  CA  . LYS A 1 238 ? 4.495   -9.941  5.186   1.00 11.35 ? 238 LYS A CA  1 
ATOM   1371 C  C   . LYS A 1 238 ? 5.649   -9.359  4.409   1.00 11.33 ? 238 LYS A C   1 
ATOM   1372 O  O   . LYS A 1 238 ? 5.473   -8.965  3.255   1.00 13.90 ? 238 LYS A O   1 
ATOM   1373 C  CB  . LYS A 1 238 ? 4.241   -11.376 4.693   1.00 12.96 ? 238 LYS A CB  1 
ATOM   1374 C  CG  . LYS A 1 238 ? 3.178   -12.116 5.490   1.00 12.48 ? 238 LYS A CG  1 
ATOM   1375 C  CD  . LYS A 1 238 ? 2.857   -13.484 4.916   1.00 13.60 ? 238 LYS A CD  1 
ATOM   1376 C  CE  . LYS A 1 238 ? 1.941   -14.311 5.792   1.00 15.63 ? 238 LYS A CE  1 
ATOM   1377 N  NZ  . LYS A 1 238 ? 1.494   -15.563 5.092   1.00 17.30 ? 238 LYS A NZ  1 
ATOM   1378 N  N   . ASP A 1 239 ? 6.814   -9.385  5.009   1.00 11.03 ? 239 ASP A N   1 
ATOM   1379 C  CA  . ASP A 1 239 ? 8.019   -8.795  4.452   1.00 11.82 ? 239 ASP A CA  1 
ATOM   1380 C  C   . ASP A 1 239 ? 9.178   -9.754  4.695   1.00 13.27 ? 239 ASP A C   1 
ATOM   1381 O  O   . ASP A 1 239 ? 9.486   -9.988  5.868   1.00 12.42 ? 239 ASP A O   1 
ATOM   1382 C  CB  . ASP A 1 239 ? 8.201   -7.385  5.047   1.00 12.61 ? 239 ASP A CB  1 
ATOM   1383 C  CG  . ASP A 1 239 ? 9.076   -6.450  4.235   1.00 14.70 ? 239 ASP A CG  1 
ATOM   1384 O  OD1 . ASP A 1 239 ? 9.782   -6.930  3.291   1.00 13.06 ? 239 ASP A OD1 1 
ATOM   1385 O  OD2 . ASP A 1 239 ? 8.883   -5.224  4.453   1.00 15.78 ? 239 ASP A OD2 1 
ATOM   1386 N  N   . GLY A 1 240 ? 9.686   -10.376 3.598   1.00 12.73 ? 240 GLY A N   1 
ATOM   1387 C  CA  . GLY A 1 240 ? 10.824  -11.282 3.626   1.00 13.75 ? 240 GLY A CA  1 
ATOM   1388 C  C   . GLY A 1 240 ? 10.543  -12.616 2.953   1.00 12.98 ? 240 GLY A C   1 
ATOM   1389 O  O   . GLY A 1 240 ? 11.352  -13.510 3.101   1.00 13.37 ? 240 GLY A O   1 
ATOM   1390 N  N   . THR A 1 241 ? 9.391   -12.761 2.299   1.00 12.71 ? 241 THR A N   1 
ATOM   1391 C  CA  . THR A 1 241 ? 9.039   -14.013 1.627   1.00 12.76 ? 241 THR A CA  1 
ATOM   1392 C  C   . THR A 1 241 ? 10.127  -14.471 0.687   1.00 13.73 ? 241 THR A C   1 
ATOM   1393 O  O   . THR A 1 241 ? 10.590  -15.612 0.774   1.00 14.37 ? 241 THR A O   1 
ATOM   1394 C  CB  . THR A 1 241 ? 7.678   -13.951 0.922   1.00 13.52 ? 241 THR A CB  1 
ATOM   1395 O  OG1 . THR A 1 241 ? 6.732   -13.609 1.934   1.00 13.66 ? 241 THR A OG1 1 
ATOM   1396 C  CG2 . THR A 1 241 ? 7.329   -15.280 0.244   1.00 14.75 ? 241 THR A CG2 1 
ATOM   1397 N  N   . ARG A 1 242 ? 10.482  -13.579 -0.268  1.00 12.05 ? 242 ARG A N   1 
ATOM   1398 C  CA  . ARG A 1 242 ? 11.456  -13.888 -1.295  1.00 12.93 ? 242 ARG A CA  1 
ATOM   1399 C  C   . ARG A 1 242 ? 12.776  -13.195 -1.010  1.00 14.82 ? 242 ARG A C   1 
ATOM   1400 O  O   . ARG A 1 242 ? 13.061  -12.189 -1.587  1.00 15.69 ? 242 ARG A O   1 
ATOM   1401 C  CB  . ARG A 1 242 ? 10.889  -13.548 -2.672  1.00 14.64 ? 242 ARG A CB  1 
ATOM   1402 C  CG  . ARG A 1 242 ? 10.139  -14.750 -3.216  1.00 15.50 ? 242 ARG A CG  1 
ATOM   1403 C  CD  . ARG A 1 242 ? 9.568   -14.636 -4.583  1.00 16.13 ? 242 ARG A CD  1 
ATOM   1404 N  NE  . ARG A 1 242 ? 10.454  -14.004 -5.494  1.00 16.42 ? 242 ARG A NE  1 
ATOM   1405 C  CZ  . ARG A 1 242 ? 11.562  -14.523 -5.962  1.00 16.53 ? 242 ARG A CZ  1 
ATOM   1406 N  NH1 . ARG A 1 242 ? 12.470  -13.709 -6.468  1.00 16.12 ? 242 ARG A NH1 1 
ATOM   1407 N  NH2 . ARG A 1 242 ? 11.726  -15.848 -5.945  1.00 17.24 ? 242 ARG A NH2 1 
ATOM   1408 N  N   . ASN A 1 243 ? 13.545  -13.761 -0.109  1.00 14.11 ? 243 ASN A N   1 
ATOM   1409 C  CA  . ASN A 1 243 ? 14.813  -13.230 0.337   1.00 14.42 ? 243 ASN A CA  1 
ATOM   1410 C  C   . ASN A 1 243 ? 15.856  -14.278 -0.034  1.00 18.35 ? 243 ASN A C   1 
ATOM   1411 O  O   . ASN A 1 243 ? 15.759  -14.898 -1.107  1.00 26.95 ? 243 ASN A O   1 
ATOM   1412 C  CB  . ASN A 1 243 ? 14.728  -12.857 1.803   1.00 14.03 ? 243 ASN A CB  1 
ATOM   1413 C  CG  . ASN A 1 243 ? 15.774  -11.876 2.258   1.00 13.54 ? 243 ASN A CG  1 
ATOM   1414 O  OD1 . ASN A 1 243 ? 16.184  -11.014 1.490   1.00 14.58 ? 243 ASN A OD1 1 
ATOM   1415 N  ND2 . ASN A 1 243 ? 16.251  -12.026 3.468   1.00 11.88 ? 243 ASN A ND2 1 
ATOM   1416 N  N   . ILE A 1 244 ? 16.980  -14.245 0.637   1.00 18.00 ? 244 ILE A N   1 
ATOM   1417 C  CA  . ILE A 1 244 ? 17.982  -15.290 0.606   1.00 16.77 ? 244 ILE A CA  1 
ATOM   1418 C  C   . ILE A 1 244 ? 17.940  -15.948 1.969   1.00 17.75 ? 244 ILE A C   1 
ATOM   1419 O  O   . ILE A 1 244 ? 17.956  -15.242 2.979   1.00 21.80 ? 244 ILE A O   1 
ATOM   1420 C  CB  . ILE A 1 244 ? 19.352  -14.702 0.216   1.00 17.85 ? 244 ILE A CB  1 
ATOM   1421 C  CG1 . ILE A 1 244 ? 19.263  -14.019 -1.148  1.00 17.15 ? 244 ILE A CG1 1 
ATOM   1422 C  CG2 . ILE A 1 244 ? 20.376  -15.825 0.178   1.00 20.49 ? 244 ILE A CG2 1 
ATOM   1423 C  CD1 . ILE A 1 244 ? 20.524  -13.354 -1.540  1.00 17.99 ? 244 ILE A CD1 1 
ATOM   1424 N  N   . ALA A 1 245 ? 17.825  -17.270 1.984   1.00 16.89 ? 245 ALA A N   1 
ATOM   1425 C  CA  . ALA A 1 245 ? 17.878  -18.058 3.197   1.00 19.81 ? 245 ALA A CA  1 
ATOM   1426 C  C   . ALA A 1 245 ? 19.331  -18.314 3.599   1.00 19.64 ? 245 ALA A C   1 
ATOM   1427 O  O   . ALA A 1 245 ? 20.231  -18.392 2.775   1.00 19.16 ? 245 ALA A O   1 
ATOM   1428 C  CB  . ALA A 1 245 ? 17.076  -19.323 3.025   1.00 21.20 ? 245 ALA A CB  1 
ATOM   1429 N  N   . GLY A 1 246 ? 19.558  -18.403 4.901   1.00 19.65 ? 246 GLY A N   1 
ATOM   1430 C  CA  . GLY A 1 246 ? 20.881  -18.645 5.464   1.00 21.91 ? 246 GLY A CA  1 
ATOM   1431 C  C   . GLY A 1 246 ? 21.430  -20.026 5.075   1.00 25.30 ? 246 GLY A C   1 
ATOM   1432 O  O   . GLY A 1 246 ? 22.649  -20.243 5.071   1.00 26.91 ? 246 GLY A O   1 
ATOM   1433 N  N   . THR A 1 247 ? 20.532  -20.929 4.676   1.00 22.77 ? 247 THR A N   1 
ATOM   1434 C  CA  . THR A 1 247 ? 20.913  -22.260 4.179   1.00 28.15 ? 247 THR A CA  1 
ATOM   1435 C  C   . THR A 1 247 ? 21.307  -22.273 2.715   1.00 27.85 ? 247 THR A C   1 
ATOM   1436 O  O   . THR A 1 247 ? 21.790  -23.304 2.257   1.00 28.20 ? 247 THR A O   1 
ATOM   1437 C  CB  . THR A 1 247 ? 19.760  -23.263 4.358   1.00 26.68 ? 247 THR A CB  1 
ATOM   1438 O  OG1 . THR A 1 247 ? 18.619  -22.672 3.747   1.00 28.23 ? 247 THR A OG1 1 
ATOM   1439 C  CG2 . THR A 1 247 ? 19.483  -23.546 5.818   1.00 32.14 ? 247 THR A CG2 1 
ATOM   1440 N  N   . GLU A 1 248 ? 21.037  -21.200 1.950   1.00 24.25 ? 248 GLU A N   1 
ATOM   1441 C  CA  . GLU A 1 248 ? 21.282  -21.224 0.501   1.00 22.18 ? 248 GLU A CA  1 
ATOM   1442 C  C   . GLU A 1 248 ? 22.700  -20.769 0.179   1.00 19.70 ? 248 GLU A C   1 
ATOM   1443 O  O   . GLU A 1 248 ? 22.876  -19.641 -0.287  1.00 23.88 ? 248 GLU A O   1 
ATOM   1444 C  CB  . GLU A 1 248 ? 20.301  -20.279 -0.180  1.00 23.48 ? 248 GLU A CB  1 
ATOM   1445 C  CG  . GLU A 1 248 ? 18.866  -20.740 -0.002  1.00 21.58 ? 248 GLU A CG  1 
ATOM   1446 C  CD  . GLU A 1 248 ? 17.768  -19.894 -0.658  1.00 24.17 ? 248 GLU A CD  1 
ATOM   1447 O  OE1 . GLU A 1 248 ? 17.768  -18.642 -0.595  1.00 21.27 ? 248 GLU A OE1 1 
ATOM   1448 O  OE2 . GLU A 1 248 ? 16.805  -20.476 -1.079  1.00 33.58 ? 248 GLU A OE2 1 
ATOM   1449 N  N   . LYS A 1 249 ? 23.690  -21.645 0.411   1.00 21.25 ? 249 LYS A N   1 
ATOM   1450 C  CA  . LYS A 1 249 ? 25.118  -21.336 0.397   1.00 21.58 ? 249 LYS A CA  1 
ATOM   1451 C  C   . LYS A 1 249 ? 25.467  -20.786 -0.981  1.00 20.34 ? 249 LYS A C   1 
ATOM   1452 O  O   . LYS A 1 249 ? 26.204  -19.814 -1.079  1.00 23.49 ? 249 LYS A O   1 
ATOM   1453 C  CB  . LYS A 1 249 ? 26.007  -22.566 0.779   1.00 20.44 ? 249 LYS A CB  1 
ATOM   1454 N  N   . ASP A 1 250 ? 24.936  -21.399 -2.045  1.00 21.10 ? 250 ASP A N   1 
ATOM   1455 C  CA  . ASP A 1 250 ? 25.156  -21.037 -3.443  1.00 25.84 ? 250 ASP A CA  1 
ATOM   1456 C  C   . ASP A 1 250 ? 24.736  -19.580 -3.729  1.00 23.96 ? 250 ASP A C   1 
ATOM   1457 O  O   . ASP A 1 250 ? 25.481  -18.787 -4.307  1.00 22.81 ? 250 ASP A O   1 
ATOM   1458 C  CB  . ASP A 1 250 ? 24.382  -22.031 -4.335  1.00 30.84 ? 250 ASP A CB  1 
ATOM   1459 N  N   . ARG A 1 251 ? 23.522  -19.215 -3.292  1.00 22.28 ? 251 ARG A N   1 
ATOM   1460 C  CA  . ARG A 1 251 ? 23.000  -17.860 -3.455  1.00 21.04 ? 251 ARG A CA  1 
ATOM   1461 C  C   . ARG A 1 251 ? 23.749  -16.815 -2.620  1.00 17.92 ? 251 ARG A C   1 
ATOM   1462 O  O   . ARG A 1 251 ? 23.932  -15.682 -3.066  1.00 18.04 ? 251 ARG A O   1 
ATOM   1463 C  CB  . ARG A 1 251 ? 21.524  -17.866 -3.052  1.00 20.28 ? 251 ARG A CB  1 
ATOM   1464 C  CG  . ARG A 1 251 ? 20.685  -18.753 -3.989  1.00 24.76 ? 251 ARG A CG  1 
ATOM   1465 C  CD  . ARG A 1 251 ? 19.211  -18.612 -3.751  1.00 25.70 ? 251 ARG A CD  1 
ATOM   1466 N  NE  . ARG A 1 251 ? 18.654  -17.433 -4.357  1.00 23.22 ? 251 ARG A NE  1 
ATOM   1467 C  CZ  . ARG A 1 251 ? 17.692  -16.711 -3.821  1.00 25.25 ? 251 ARG A CZ  1 
ATOM   1468 N  NH1 . ARG A 1 251 ? 17.156  -16.972 -2.623  1.00 24.24 ? 251 ARG A NH1 1 
ATOM   1469 N  NH2 . ARG A 1 251 ? 17.209  -15.765 -4.572  1.00 25.29 ? 251 ARG A NH2 1 
ATOM   1470 N  N   . LEU A 1 252 ? 24.215  -17.197 -1.449  1.00 17.43 ? 252 LEU A N   1 
ATOM   1471 C  CA  . LEU A 1 252 ? 24.997  -16.316 -0.607  1.00 19.59 ? 252 LEU A CA  1 
ATOM   1472 C  C   . LEU A 1 252 ? 26.328  -16.012 -1.282  1.00 19.00 ? 252 LEU A C   1 
ATOM   1473 O  O   . LEU A 1 252 ? 26.786  -14.872 -1.309  1.00 17.61 ? 252 LEU A O   1 
ATOM   1474 C  CB  . LEU A 1 252 ? 25.175  -16.971 0.762   1.00 19.24 ? 252 LEU A CB  1 
ATOM   1475 C  CG  . LEU A 1 252 ? 23.920  -16.993 1.642   1.00 21.66 ? 252 LEU A CG  1 
ATOM   1476 C  CD1 . LEU A 1 252 ? 24.129  -17.861 2.856   1.00 23.48 ? 252 LEU A CD1 1 
ATOM   1477 C  CD2 . LEU A 1 252 ? 23.522  -15.580 2.070   1.00 26.69 ? 252 LEU A CD2 1 
ATOM   1478 N  N   . ASP A 1 253 ? 26.997  -17.065 -1.809  1.00 18.43 ? 253 ASP A N   1 
ATOM   1479 C  CA  . ASP A 1 253 ? 28.251  -16.868 -2.540  1.00 20.18 ? 253 ASP A CA  1 
ATOM   1480 C  C   . ASP A 1 253 ? 28.065  -15.959 -3.754  1.00 20.26 ? 253 ASP A C   1 
ATOM   1481 O  O   . ASP A 1 253 ? 28.940  -15.138 -4.060  1.00 21.45 ? 253 ASP A O   1 
ATOM   1482 C  CB  . ASP A 1 253 ? 28.811  -18.242 -2.912  1.00 21.26 ? 253 ASP A CB  1 
ATOM   1483 C  CG  . ASP A 1 253 ? 29.481  -18.917 -1.722  1.00 23.79 ? 253 ASP A CG  1 
ATOM   1484 O  OD1 . ASP A 1 253 ? 29.793  -18.266 -0.724  1.00 26.54 ? 253 ASP A OD1 1 
ATOM   1485 O  OD2 . ASP A 1 253 ? 29.631  -20.150 -1.775  1.00 31.54 ? 253 ASP A OD2 1 
ATOM   1486 N  N   . ARG A 1 254 ? 26.951  -16.138 -4.480  1.00 19.90 ? 254 ARG A N   1 
ATOM   1487 C  CA  . ARG A 1 254 ? 26.667  -15.397 -5.695  1.00 21.06 ? 254 ARG A CA  1 
ATOM   1488 C  C   . ARG A 1 254 ? 26.300  -13.941 -5.414  1.00 18.12 ? 254 ARG A C   1 
ATOM   1489 O  O   . ARG A 1 254 ? 26.732  -13.022 -6.087  1.00 18.06 ? 254 ARG A O   1 
ATOM   1490 C  CB  . ARG A 1 254 ? 25.520  -16.071 -6.472  1.00 25.05 ? 254 ARG A CB  1 
ATOM   1491 C  CG  . ARG A 1 254 ? 25.370  -15.635 -7.929  1.00 30.90 ? 254 ARG A CG  1 
ATOM   1492 C  CD  . ARG A 1 254 ? 24.513  -16.631 -8.715  1.00 31.58 ? 254 ARG A CD  1 
ATOM   1493 N  N   . PHE A 1 255 ? 25.539  -13.692 -4.340  1.00 18.02 ? 255 PHE A N   1 
ATOM   1494 C  CA  . PHE A 1 255 ? 24.886  -12.410 -4.218  1.00 16.24 ? 255 PHE A CA  1 
ATOM   1495 C  C   . PHE A 1 255 ? 25.268  -11.618 -2.964  1.00 16.19 ? 255 PHE A C   1 
ATOM   1496 O  O   . PHE A 1 255 ? 24.962  -10.431 -2.893  1.00 19.00 ? 255 PHE A O   1 
ATOM   1497 C  CB  . PHE A 1 255 ? 23.376  -12.581 -4.148  1.00 18.29 ? 255 PHE A CB  1 
ATOM   1498 C  CG  . PHE A 1 255 ? 22.808  -13.100 -5.440  1.00 19.28 ? 255 PHE A CG  1 
ATOM   1499 C  CD1 . PHE A 1 255 ? 22.886  -12.343 -6.592  1.00 20.13 ? 255 PHE A CD1 1 
ATOM   1500 C  CD2 . PHE A 1 255 ? 22.168  -14.323 -5.478  1.00 20.52 ? 255 PHE A CD2 1 
ATOM   1501 C  CE1 . PHE A 1 255 ? 22.328  -12.848 -7.768  1.00 21.48 ? 255 PHE A CE1 1 
ATOM   1502 C  CE2 . PHE A 1 255 ? 21.651  -14.850 -6.660  1.00 24.73 ? 255 PHE A CE2 1 
ATOM   1503 C  CZ  . PHE A 1 255 ? 21.702  -14.075 -7.777  1.00 22.04 ? 255 PHE A CZ  1 
ATOM   1504 N  N   . VAL A 1 256 ? 25.912  -12.261 -1.984  1.00 15.25 ? 256 VAL A N   1 
ATOM   1505 C  CA  . VAL A 1 256 ? 26.127  -11.605 -0.700  1.00 16.34 ? 256 VAL A CA  1 
ATOM   1506 C  C   . VAL A 1 256 ? 27.589  -11.409 -0.368  1.00 14.65 ? 256 VAL A C   1 
ATOM   1507 O  O   . VAL A 1 256 ? 27.976  -10.330 0.063   1.00 18.08 ? 256 VAL A O   1 
ATOM   1508 C  CB  . VAL A 1 256 ? 25.373  -12.360 0.404   1.00 16.11 ? 256 VAL A CB  1 
ATOM   1509 C  CG1 . VAL A 1 256 ? 25.710  -11.837 1.776   1.00 17.26 ? 256 VAL A CG1 1 
ATOM   1510 C  CG2 . VAL A 1 256 ? 23.870  -12.308 0.120   1.00 19.53 ? 256 VAL A CG2 1 
ATOM   1511 N  N   . TRP A 1 257 ? 28.381  -12.478 -0.447  1.00 17.62 ? 257 TRP A N   1 
ATOM   1512 C  CA  . TRP A 1 257 ? 29.747  -12.447 0.013   1.00 16.82 ? 257 TRP A CA  1 
ATOM   1513 C  C   . TRP A 1 257 ? 30.655  -11.902 -1.068  1.00 20.90 ? 257 TRP A C   1 
ATOM   1514 O  O   . TRP A 1 257 ? 30.633  -12.401 -2.194  1.00 22.09 ? 257 TRP A O   1 
ATOM   1515 C  CB  . TRP A 1 257 ? 30.237  -13.849 0.428   1.00 17.93 ? 257 TRP A CB  1 
ATOM   1516 C  CG  . TRP A 1 257 ? 29.405  -14.543 1.460   1.00 18.16 ? 257 TRP A CG  1 
ATOM   1517 C  CD1 . TRP A 1 257 ? 28.903  -15.795 1.380   1.00 19.76 ? 257 TRP A CD1 1 
ATOM   1518 C  CD2 . TRP A 1 257 ? 28.929  -14.002 2.720   1.00 19.78 ? 257 TRP A CD2 1 
ATOM   1519 N  NE1 . TRP A 1 257 ? 28.185  -16.095 2.511   1.00 23.17 ? 257 TRP A NE1 1 
ATOM   1520 C  CE2 . TRP A 1 257 ? 28.201  -15.021 3.358   1.00 19.25 ? 257 TRP A CE2 1 
ATOM   1521 C  CE3 . TRP A 1 257 ? 29.110  -12.779 3.379   1.00 20.77 ? 257 TRP A CE3 1 
ATOM   1522 C  CZ2 . TRP A 1 257 ? 27.597  -14.831 4.607   1.00 20.96 ? 257 TRP A CZ2 1 
ATOM   1523 C  CZ3 . TRP A 1 257 ? 28.559  -12.610 4.642   1.00 20.65 ? 257 TRP A CZ3 1 
ATOM   1524 C  CH2 . TRP A 1 257 ? 27.765  -13.594 5.209   1.00 20.28 ? 257 TRP A CH2 1 
ATOM   1525 N  N   . ALA A 1 258 ? 31.570  -11.021 -0.669  1.00 18.69 ? 258 ALA A N   1 
ATOM   1526 C  CA  . ALA A 1 258 ? 32.636  -10.585 -1.545  1.00 19.95 ? 258 ALA A CA  1 
ATOM   1527 C  C   . ALA A 1 258 ? 33.629  -11.726 -1.797  1.00 19.54 ? 258 ALA A C   1 
ATOM   1528 O  O   . ALA A 1 258 ? 34.005  -12.479 -0.888  1.00 18.48 ? 258 ALA A O   1 
ATOM   1529 C  CB  . ALA A 1 258 ? 33.308  -9.353  -0.964  1.00 20.69 ? 258 ALA A CB  1 
ATOM   1530 N  N   . ALA A 1 259 ? 34.037  -11.861 -3.068  1.00 23.56 ? 259 ALA A N   1 
ATOM   1531 C  CA  . ALA A 1 259 ? 34.964  -12.907 -3.491  1.00 25.20 ? 259 ALA A CA  1 
ATOM   1532 C  C   . ALA A 1 259 ? 36.341  -12.279 -3.723  1.00 27.59 ? 259 ALA A C   1 
ATOM   1533 O  O   . ALA A 1 259 ? 36.419  -11.112 -4.070  1.00 24.39 ? 259 ALA A O   1 
ATOM   1534 C  CB  . ALA A 1 259 ? 34.402  -13.544 -4.721  1.00 27.07 ? 259 ALA A CB  1 
ATOM   1535 N  N   . GLU A 1 260 ? 37.438  -13.056 -3.596  1.00 29.07 ? 260 GLU A N   1 
ATOM   1536 C  CA  . GLU A 1 260 ? 38.760  -12.501 -3.869  1.00 32.45 ? 260 GLU A CA  1 
ATOM   1537 C  C   . GLU A 1 260 ? 38.823  -11.847 -5.249  1.00 29.07 ? 260 GLU A C   1 
ATOM   1538 O  O   . GLU A 1 260 ? 39.359  -10.734 -5.390  1.00 32.05 ? 260 GLU A O   1 
ATOM   1539 C  CB  . GLU A 1 260 ? 39.861  -13.555 -3.820  1.00 36.38 ? 260 GLU A CB  1 
ATOM   1540 C  CG  . GLU A 1 260 ? 41.236  -12.900 -3.956  1.00 44.25 ? 260 GLU A CG  1 
ATOM   1541 C  CD  . GLU A 1 260 ? 42.385  -13.727 -3.437  1.00 48.29 ? 260 GLU A CD  1 
ATOM   1542 O  OE1 . GLU A 1 260 ? 42.226  -14.976 -3.344  1.00 45.04 ? 260 GLU A OE1 1 
ATOM   1543 O  OE2 . GLU A 1 260 ? 43.410  -13.101 -3.077  1.00 54.79 ? 260 GLU A OE2 1 
ATOM   1544 N  N   . LYS A 1 261 ? 38.225  -12.516 -6.235  1.00 31.16 ? 261 LYS A N   1 
ATOM   1545 C  CA  . LYS A 1 261 ? 38.334  -12.087 -7.628  1.00 34.53 ? 261 LYS A CA  1 
ATOM   1546 C  C   . LYS A 1 261 ? 37.624  -10.757 -7.854  1.00 33.76 ? 261 LYS A C   1 
ATOM   1547 O  O   . LYS A 1 261 ? 37.818  -10.138 -8.886  1.00 27.58 ? 261 LYS A O   1 
ATOM   1548 C  CB  . LYS A 1 261 ? 37.816  -13.149 -8.622  1.00 40.96 ? 261 LYS A CB  1 
ATOM   1549 C  CG  . LYS A 1 261 ? 36.308  -13.332 -8.794  1.00 40.81 ? 261 LYS A CG  1 
ATOM   1550 N  N   . ASP A 1 262 ? 36.821  -10.274 -6.888  1.00 30.43 ? 262 ASP A N   1 
ATOM   1551 C  CA  . ASP A 1 262 ? 36.055  -9.063  -7.108  1.00 27.32 ? 262 ASP A CA  1 
ATOM   1552 C  C   . ASP A 1 262 ? 36.950  -7.837  -7.013  1.00 27.92 ? 262 ASP A C   1 
ATOM   1553 O  O   . ASP A 1 262 ? 36.537  -6.710  -7.297  1.00 30.75 ? 262 ASP A O   1 
ATOM   1554 C  CB  . ASP A 1 262 ? 34.895  -8.914  -6.108  1.00 26.39 ? 262 ASP A CB  1 
ATOM   1555 C  CG  . ASP A 1 262 ? 33.833  -9.993  -6.220  1.00 25.76 ? 262 ASP A CG  1 
ATOM   1556 O  OD1 . ASP A 1 262 ? 33.787  -10.697 -7.241  1.00 20.87 ? 262 ASP A OD1 1 
ATOM   1557 O  OD2 . ASP A 1 262 ? 33.075  -10.176 -5.216  1.00 21.28 ? 262 ASP A OD2 1 
ATOM   1558 N  N   . GLY A 1 263 ? 38.167  -7.973  -6.520  1.00 32.23 ? 263 GLY A N   1 
ATOM   1559 C  CA  . GLY A 1 263 ? 39.068  -6.844  -6.700  1.00 30.53 ? 263 GLY A CA  1 
ATOM   1560 C  C   . GLY A 1 263 ? 39.663  -6.299  -5.419  1.00 35.28 ? 263 GLY A C   1 
ATOM   1561 O  O   . GLY A 1 263 ? 40.528  -5.444  -5.513  1.00 35.45 ? 263 GLY A O   1 
ATOM   1562 N  N   . THR A 1 264 ? 39.107  -6.658  -4.249  1.00 25.70 ? 264 THR A N   1 
ATOM   1563 C  CA  . THR A 1 264 ? 39.592  -6.096  -2.993  1.00 23.63 ? 264 THR A CA  1 
ATOM   1564 C  C   . THR A 1 264 ? 39.890  -7.239  -2.057  1.00 27.47 ? 264 THR A C   1 
ATOM   1565 O  O   . THR A 1 264 ? 38.963  -7.792  -1.449  1.00 25.46 ? 264 THR A O   1 
ATOM   1566 C  CB  . THR A 1 264 ? 38.594  -5.136  -2.326  1.00 26.45 ? 264 THR A CB  1 
ATOM   1567 O  OG1 . THR A 1 264 ? 38.099  -4.172  -3.273  1.00 29.86 ? 264 THR A OG1 1 
ATOM   1568 C  CG2 . THR A 1 264 ? 39.242  -4.438  -1.158  1.00 27.39 ? 264 THR A CG2 1 
ATOM   1569 N  N   . PRO A 1 265 ? 41.141  -7.740  -2.017  1.00 23.93 ? 265 PRO A N   1 
ATOM   1570 C  CA  . PRO A 1 265 ? 41.407  -8.963  -1.264  1.00 26.21 ? 265 PRO A CA  1 
ATOM   1571 C  C   . PRO A 1 265 ? 41.047  -8.909  0.231   1.00 20.76 ? 265 PRO A C   1 
ATOM   1572 O  O   . PRO A 1 265 ? 40.656  -9.936  0.777   1.00 21.52 ? 265 PRO A O   1 
ATOM   1573 C  CB  . PRO A 1 265 ? 42.911  -9.222  -1.512  1.00 29.69 ? 265 PRO A CB  1 
ATOM   1574 C  CG  . PRO A 1 265 ? 43.243  -8.443  -2.801  1.00 28.58 ? 265 PRO A CG  1 
ATOM   1575 C  CD  . PRO A 1 265 ? 42.283  -7.267  -2.813  1.00 28.67 ? 265 PRO A CD  1 
ATOM   1576 N  N   . TRP A 1 266 ? 41.254  -7.785  0.905   1.00 23.10 ? 266 TRP A N   1 
ATOM   1577 C  CA  . TRP A 1 266 ? 40.942  -7.684  2.332   1.00 22.55 ? 266 TRP A CA  1 
ATOM   1578 C  C   . TRP A 1 266 ? 39.454  -7.890  2.627   1.00 21.40 ? 266 TRP A C   1 
ATOM   1579 O  O   . TRP A 1 266 ? 39.090  -8.269  3.742   1.00 21.92 ? 266 TRP A O   1 
ATOM   1580 C  CB  . TRP A 1 266 ? 41.491  -6.382  2.927   1.00 22.30 ? 266 TRP A CB  1 
ATOM   1581 C  CG  . TRP A 1 266 ? 40.736  -5.131  2.633   1.00 22.86 ? 266 TRP A CG  1 
ATOM   1582 C  CD1 . TRP A 1 266 ? 41.047  -4.207  1.696   1.00 21.51 ? 266 TRP A CD1 1 
ATOM   1583 C  CD2 . TRP A 1 266 ? 39.569  -4.628  3.334   1.00 22.54 ? 266 TRP A CD2 1 
ATOM   1584 N  NE1 . TRP A 1 266 ? 40.172  -3.173  1.770   1.00 24.95 ? 266 TRP A NE1 1 
ATOM   1585 C  CE2 . TRP A 1 266 ? 39.258  -3.383  2.772   1.00 20.13 ? 266 TRP A CE2 1 
ATOM   1586 C  CE3 . TRP A 1 266 ? 38.810  -5.058  4.445   1.00 21.91 ? 266 TRP A CE3 1 
ATOM   1587 C  CZ2 . TRP A 1 266 ? 38.184  -2.612  3.188   1.00 20.45 ? 266 TRP A CZ2 1 
ATOM   1588 C  CZ3 . TRP A 1 266 ? 37.772  -4.275  4.880   1.00 20.58 ? 266 TRP A CZ3 1 
ATOM   1589 C  CH2 . TRP A 1 266 ? 37.425  -3.096  4.227   1.00 19.82 ? 266 TRP A CH2 1 
ATOM   1590 N  N   . MET A 1 267 ? 38.595  -7.701  1.600   1.00 20.95 ? 267 MET A N   1 
ATOM   1591 C  CA  . MET A 1 267 ? 37.165  -7.837  1.772   1.00 20.65 ? 267 MET A CA  1 
ATOM   1592 C  C   . MET A 1 267 ? 36.664  -9.241  1.509   1.00 21.34 ? 267 MET A C   1 
ATOM   1593 O  O   . MET A 1 267 ? 35.475  -9.432  1.655   1.00 18.95 ? 267 MET A O   1 
ATOM   1594 C  CB  . MET A 1 267 ? 36.416  -6.818  0.891   1.00 20.12 ? 267 MET A CB  1 
ATOM   1595 C  CG  . MET A 1 267 ? 36.178  -5.492  1.625   1.00 19.76 ? 267 MET A CG  1 
ATOM   1596 S  SD  . MET A 1 267 ? 35.091  -5.675  3.052   1.00 18.69 ? 267 MET A SD  1 
ATOM   1597 C  CE  . MET A 1 267 ? 33.577  -6.146  2.201   1.00 19.49 ? 267 MET A CE  1 
ATOM   1598 N  N   . THR A 1 268 ? 37.525  -10.217 1.110   1.00 22.33 ? 268 THR A N   1 
ATOM   1599 C  CA  . THR A 1 268 ? 37.072  -11.554 0.803   1.00 20.54 ? 268 THR A CA  1 
ATOM   1600 C  C   . THR A 1 268 ? 36.342  -12.173 2.001   1.00 19.30 ? 268 THR A C   1 
ATOM   1601 O  O   . THR A 1 268 ? 36.915  -12.269 3.072   1.00 20.31 ? 268 THR A O   1 
ATOM   1602 C  CB  . THR A 1 268 ? 38.253  -12.455 0.403   1.00 23.12 ? 268 THR A CB  1 
ATOM   1603 O  OG1 . THR A 1 268 ? 38.830  -11.832 -0.764  1.00 24.61 ? 268 THR A OG1 1 
ATOM   1604 C  CG2 . THR A 1 268 ? 37.804  -13.863 0.092   1.00 25.94 ? 268 THR A CG2 1 
ATOM   1605 N  N   . GLY A 1 269 ? 35.118  -12.627 1.801   1.00 16.72 ? 269 GLY A N   1 
ATOM   1606 C  CA  . GLY A 1 269 ? 34.297  -13.174 2.862   1.00 18.63 ? 269 GLY A CA  1 
ATOM   1607 C  C   . GLY A 1 269 ? 33.437  -12.128 3.582   1.00 17.07 ? 269 GLY A C   1 
ATOM   1608 O  O   . GLY A 1 269 ? 32.655  -12.520 4.417   1.00 16.76 ? 269 GLY A O   1 
ATOM   1609 N  N   . GLY A 1 270 ? 33.647  -10.831 3.325   1.00 15.09 ? 270 GLY A N   1 
ATOM   1610 C  CA  . GLY A 1 270 ? 32.787  -9.770  3.836   1.00 14.96 ? 270 GLY A CA  1 
ATOM   1611 C  C   . GLY A 1 270 ? 31.593  -9.504  2.939   1.00 13.59 ? 270 GLY A C   1 
ATOM   1612 O  O   . GLY A 1 270 ? 31.270  -10.327 2.078   1.00 16.68 ? 270 GLY A O   1 
ATOM   1613 N  N   . SER A 1 271 ? 30.894  -8.390  3.205   1.00 15.58 ? 271 SER A N   1 
ATOM   1614 C  CA  . SER A 1 271 ? 29.701  -8.036  2.446   1.00 14.96 ? 271 SER A CA  1 
ATOM   1615 C  C   . SER A 1 271 ? 29.592  -6.526  2.452   1.00 16.96 ? 271 SER A C   1 
ATOM   1616 O  O   . SER A 1 271 ? 30.372  -5.863  3.080   1.00 20.47 ? 271 SER A O   1 
ATOM   1617 C  CB  . SER A 1 271 ? 28.446  -8.699  3.004   1.00 15.47 ? 271 SER A CB  1 
ATOM   1618 O  OG  . SER A 1 271 ? 27.392  -8.650  2.067   1.00 15.95 ? 271 SER A OG  1 
ATOM   1619 N  N   . TYR A 1 272 ? 28.633  -5.951  1.742   1.00 15.14 ? 272 TYR A N   1 
ATOM   1620 C  CA  . TYR A 1 272 ? 28.424  -4.533  1.749   1.00 14.32 ? 272 TYR A CA  1 
ATOM   1621 C  C   . TYR A 1 272 ? 26.993  -4.275  2.170   1.00 13.98 ? 272 TYR A C   1 
ATOM   1622 O  O   . TYR A 1 272 ? 26.108  -5.022  1.776   1.00 13.73 ? 272 TYR A O   1 
ATOM   1623 C  CB  . TYR A 1 272 ? 28.628  -3.918  0.350   1.00 15.27 ? 272 TYR A CB  1 
ATOM   1624 C  CG  . TYR A 1 272 ? 30.040  -4.108  -0.118  1.00 16.09 ? 272 TYR A CG  1 
ATOM   1625 C  CD1 . TYR A 1 272 ? 31.017  -3.194  0.283   1.00 16.79 ? 272 TYR A CD1 1 
ATOM   1626 C  CD2 . TYR A 1 272 ? 30.445  -5.280  -0.732  1.00 16.39 ? 272 TYR A CD2 1 
ATOM   1627 C  CE1 . TYR A 1 272 ? 32.341  -3.385  -0.082  1.00 17.82 ? 272 TYR A CE1 1 
ATOM   1628 C  CE2 . TYR A 1 272 ? 31.792  -5.544  -0.992  1.00 17.43 ? 272 TYR A CE2 1 
ATOM   1629 C  CZ  . TYR A 1 272 ? 32.729  -4.554  -0.693  1.00 19.93 ? 272 TYR A CZ  1 
ATOM   1630 O  OH  . TYR A 1 272 ? 34.030  -4.737  -1.042  1.00 21.11 ? 272 TYR A OH  1 
ATOM   1631 N  N   . LEU A 1 273 ? 26.845  -3.267  3.011   1.00 14.20 ? 273 LEU A N   1 
ATOM   1632 C  CA  . LEU A 1 273 ? 25.568  -2.979  3.666   1.00 13.55 ? 273 LEU A CA  1 
ATOM   1633 C  C   . LEU A 1 273 ? 25.093  -1.600  3.244   1.00 14.63 ? 273 LEU A C   1 
ATOM   1634 O  O   . LEU A 1 273 ? 25.850  -0.635  3.297   1.00 13.56 ? 273 LEU A O   1 
ATOM   1635 C  CB  . LEU A 1 273 ? 25.853  -2.898  5.166   1.00 13.42 ? 273 LEU A CB  1 
ATOM   1636 C  CG  . LEU A 1 273 ? 24.699  -2.508  6.083   1.00 14.24 ? 273 LEU A CG  1 
ATOM   1637 C  CD1 . LEU A 1 273 ? 23.464  -3.384  5.868   1.00 15.28 ? 273 LEU A CD1 1 
ATOM   1638 C  CD2 . LEU A 1 273 ? 25.156  -2.628  7.526   1.00 16.27 ? 273 LEU A CD2 1 
ATOM   1639 N  N   . VAL A 1 274 ? 23.821  -1.531  2.881   1.00 14.01 ? 274 VAL A N   1 
ATOM   1640 C  CA  . VAL A 1 274 ? 23.090  -0.291  2.734   1.00 13.32 ? 274 VAL A CA  1 
ATOM   1641 C  C   . VAL A 1 274 ? 22.061  -0.235  3.850   1.00 13.32 ? 274 VAL A C   1 
ATOM   1642 O  O   . VAL A 1 274 ? 21.258  -1.171  4.035   1.00 14.12 ? 274 VAL A O   1 
ATOM   1643 C  CB  . VAL A 1 274 ? 22.428  -0.225  1.339   1.00 14.81 ? 274 VAL A CB  1 
ATOM   1644 C  CG1 . VAL A 1 274 ? 21.464  0.950   1.245   1.00 15.08 ? 274 VAL A CG1 1 
ATOM   1645 C  CG2 . VAL A 1 274 ? 23.433  -0.270  0.202   1.00 16.83 ? 274 VAL A CG2 1 
ATOM   1646 N  N   . ALA A 1 275 ? 22.026  0.884   4.546   1.00 12.63 ? 275 ALA A N   1 
ATOM   1647 C  CA  . ALA A 1 275 ? 20.985  1.216   5.481   1.00 14.55 ? 275 ALA A CA  1 
ATOM   1648 C  C   . ALA A 1 275 ? 20.193  2.427   5.004   1.00 16.45 ? 275 ALA A C   1 
ATOM   1649 O  O   . ALA A 1 275 ? 20.756  3.408   4.557   1.00 16.73 ? 275 ALA A O   1 
ATOM   1650 C  CB  . ALA A 1 275 ? 21.646  1.562   6.802   1.00 14.71 ? 275 ALA A CB  1 
ATOM   1651 N  N   . ARG A 1 276 ? 18.875  2.285   5.007   1.00 13.44 ? 276 ARG A N   1 
ATOM   1652 C  CA  . ARG A 1 276 ? 17.989  3.368   4.651   1.00 13.82 ? 276 ARG A CA  1 
ATOM   1653 C  C   . ARG A 1 276 ? 16.917  3.476   5.716   1.00 14.38 ? 276 ARG A C   1 
ATOM   1654 O  O   . ARG A 1 276 ? 16.204  2.543   6.013   1.00 15.04 ? 276 ARG A O   1 
ATOM   1655 C  CB  . ARG A 1 276 ? 17.326  3.149   3.296   1.00 13.43 ? 276 ARG A CB  1 
ATOM   1656 C  CG  . ARG A 1 276 ? 18.291  2.974   2.128   1.00 15.14 ? 276 ARG A CG  1 
ATOM   1657 C  CD  . ARG A 1 276 ? 18.995  4.229   1.695   1.00 16.47 ? 276 ARG A CD  1 
ATOM   1658 N  NE  . ARG A 1 276 ? 18.069  5.054   0.939   1.00 16.19 ? 276 ARG A NE  1 
ATOM   1659 C  CZ  . ARG A 1 276 ? 18.385  6.074   0.167   1.00 18.45 ? 276 ARG A CZ  1 
ATOM   1660 N  NH1 . ARG A 1 276 ? 19.668  6.439   0.046   1.00 17.45 ? 276 ARG A NH1 1 
ATOM   1661 N  NH2 . ARG A 1 276 ? 17.403  6.719   -0.481  1.00 21.30 ? 276 ARG A NH2 1 
ATOM   1662 N  N   . ARG A 1 277 ? 16.807  4.670   6.322   1.00 13.55 ? 277 ARG A N   1 
ATOM   1663 C  CA  . ARG A 1 277 ? 15.758  4.934   7.267   1.00 12.83 ? 277 ARG A CA  1 
ATOM   1664 C  C   . ARG A 1 277 ? 14.594  5.451   6.441   1.00 14.37 ? 277 ARG A C   1 
ATOM   1665 O  O   . ARG A 1 277 ? 14.768  6.448   5.754   1.00 13.56 ? 277 ARG A O   1 
ATOM   1666 C  CB  . ARG A 1 277 ? 16.267  5.973   8.279   1.00 16.62 ? 277 ARG A CB  1 
ATOM   1667 C  CG  . ARG A 1 277 ? 15.331  6.196   9.440   1.00 17.62 ? 277 ARG A CG  1 
ATOM   1668 C  CD  . ARG A 1 277 ? 16.028  7.154   10.419  1.00 27.26 ? 277 ARG A CD  1 
ATOM   1669 N  NE  . ARG A 1 277 ? 15.222  7.126   11.636  1.00 37.62 ? 277 ARG A NE  1 
ATOM   1670 C  CZ  . ARG A 1 277 ? 14.258  7.981   11.941  1.00 44.07 ? 277 ARG A CZ  1 
ATOM   1671 N  NH1 . ARG A 1 277 ? 13.989  8.981   11.111  1.00 42.71 ? 277 ARG A NH1 1 
ATOM   1672 N  NH2 . ARG A 1 277 ? 13.634  7.853   13.104  1.00 38.97 ? 277 ARG A NH2 1 
ATOM   1673 N  N   . ILE A 1 278 ? 13.446  4.752   6.496   1.00 13.35 ? 278 ILE A N   1 
ATOM   1674 C  CA  . ILE A 1 278 ? 12.319  5.076   5.654   1.00 13.53 ? 278 ILE A CA  1 
ATOM   1675 C  C   . ILE A 1 278 ? 11.085  5.361   6.522   1.00 14.81 ? 278 ILE A C   1 
ATOM   1676 O  O   . ILE A 1 278 ? 10.609  4.516   7.294   1.00 15.75 ? 278 ILE A O   1 
ATOM   1677 C  CB  . ILE A 1 278 ? 12.045  3.878   4.700   1.00 13.27 ? 278 ILE A CB  1 
ATOM   1678 C  CG1 . ILE A 1 278 ? 13.279  3.471   3.901   1.00 15.80 ? 278 ILE A CG1 1 
ATOM   1679 C  CG2 . ILE A 1 278 ? 10.874  4.236   3.818   1.00 13.41 ? 278 ILE A CG2 1 
ATOM   1680 C  CD1 . ILE A 1 278 ? 13.112  2.292   2.992   1.00 15.32 ? 278 ILE A CD1 1 
ATOM   1681 N  N   . ARG A 1 279 ? 10.567  6.589   6.449   1.00 13.27 ? 279 ARG A N   1 
ATOM   1682 C  CA  . ARG A 1 279 ? 9.368   6.952   7.144   1.00 13.96 ? 279 ARG A CA  1 
ATOM   1683 C  C   . ARG A 1 279 ? 8.178   6.468   6.310   1.00 16.10 ? 279 ARG A C   1 
ATOM   1684 O  O   . ARG A 1 279 ? 8.232   6.469   5.060   1.00 15.79 ? 279 ARG A O   1 
ATOM   1685 C  CB  . ARG A 1 279 ? 9.334   8.470   7.302   1.00 18.61 ? 279 ARG A CB  1 
ATOM   1686 C  CG  . ARG A 1 279 ? 7.996   9.065   7.737   1.00 27.68 ? 279 ARG A CG  1 
ATOM   1687 C  CD  . ARG A 1 279 ? 8.006   10.572  8.071   1.00 31.89 ? 279 ARG A CD  1 
ATOM   1688 N  NE  . ARG A 1 279 ? 8.922   10.881  9.183   1.00 40.90 ? 279 ARG A NE  1 
ATOM   1689 C  CZ  . ARG A 1 279 ? 9.972   11.721  9.100   1.00 49.26 ? 279 ARG A CZ  1 
ATOM   1690 N  NH1 . ARG A 1 279 ? 10.075  12.597  8.113   1.00 55.86 ? 279 ARG A NH1 1 
ATOM   1691 N  NH2 . ARG A 1 279 ? 10.905  11.724  10.031  1.00 45.75 ? 279 ARG A NH2 1 
ATOM   1692 N  N   . MET A 1 280 ? 7.136   5.998   7.021   1.00 12.47 ? 280 MET A N   1 
ATOM   1693 C  CA  . MET A 1 280 ? 5.910   5.547   6.356   1.00 15.44 ? 280 MET A CA  1 
ATOM   1694 C  C   . MET A 1 280 ? 4.846   6.597   6.619   1.00 16.97 ? 280 MET A C   1 
ATOM   1695 O  O   . MET A 1 280 ? 4.699   7.014   7.769   1.00 16.65 ? 280 MET A O   1 
ATOM   1696 C  CB  . MET A 1 280 ? 5.457   4.156   6.852   1.00 16.47 ? 280 MET A CB  1 
ATOM   1697 C  CG  . MET A 1 280 ? 6.424   3.075   6.485   1.00 20.14 ? 280 MET A CG  1 
ATOM   1698 S  SD  . MET A 1 280 ? 6.008   1.609   7.466   1.00 23.42 ? 280 MET A SD  1 
ATOM   1699 C  CE  . MET A 1 280 ? 6.689   0.433   6.320   1.00 25.94 ? 280 MET A CE  1 
ATOM   1700 N  N   . HIS A 1 281 ? 4.098   6.995   5.563   1.00 15.20 ? 281 HIS A N   1 
ATOM   1701 C  CA  . HIS A 1 281 ? 2.955   7.884   5.723   1.00 14.80 ? 281 HIS A CA  1 
ATOM   1702 C  C   . HIS A 1 281 ? 1.727   7.086   6.132   1.00 13.05 ? 281 HIS A C   1 
ATOM   1703 O  O   . HIS A 1 281 ? 0.933   6.679   5.263   1.00 15.12 ? 281 HIS A O   1 
ATOM   1704 C  CB  . HIS A 1 281 ? 2.754   8.617   4.396   1.00 15.29 ? 281 HIS A CB  1 
ATOM   1705 C  CG  . HIS A 1 281 ? 3.915   9.433   3.953   1.00 16.39 ? 281 HIS A CG  1 
ATOM   1706 N  ND1 . HIS A 1 281 ? 4.428   9.523   2.659   1.00 17.85 ? 281 HIS A ND1 1 
ATOM   1707 C  CD2 . HIS A 1 281 ? 4.744   10.091  4.791   1.00 15.27 ? 281 HIS A CD2 1 
ATOM   1708 C  CE1 . HIS A 1 281 ? 5.558   10.232  2.743   1.00 16.20 ? 281 HIS A CE1 1 
ATOM   1709 N  NE2 . HIS A 1 281 ? 5.754   10.626  4.032   1.00 21.72 ? 281 HIS A NE2 1 
ATOM   1710 N  N   . ILE A 1 282 ? 1.657   6.659   7.372   1.00 14.68 ? 282 ILE A N   1 
ATOM   1711 C  CA  . ILE A 1 282 ? 0.611   5.748   7.803   1.00 15.35 ? 282 ILE A CA  1 
ATOM   1712 C  C   . ILE A 1 282 ? -0.785  6.374   7.710   1.00 13.82 ? 282 ILE A C   1 
ATOM   1713 O  O   . ILE A 1 282 ? -1.744  5.664   7.414   1.00 14.20 ? 282 ILE A O   1 
ATOM   1714 C  CB  . ILE A 1 282 ? 0.837   5.077   9.161   1.00 20.68 ? 282 ILE A CB  1 
ATOM   1715 C  CG1 . ILE A 1 282 ? 0.997   6.048   10.300  1.00 24.31 ? 282 ILE A CG1 1 
ATOM   1716 C  CG2 . ILE A 1 282 ? 1.997   4.049   9.098   1.00 23.80 ? 282 ILE A CG2 1 
ATOM   1717 C  CD1 . ILE A 1 282 ? 0.818   5.346   11.660  1.00 33.53 ? 282 ILE A CD1 1 
ATOM   1718 N  N   . GLU A 1 283 ? -0.961  7.675   7.998   1.00 14.48 ? 283 GLU A N   1 
ATOM   1719 C  CA  . GLU A 1 283 ? -2.246  8.328   7.763   1.00 12.86 ? 283 GLU A CA  1 
ATOM   1720 C  C   . GLU A 1 283 ? -2.753  8.077   6.335   1.00 13.98 ? 283 GLU A C   1 
ATOM   1721 O  O   . GLU A 1 283 ? -3.861  7.644   6.100   1.00 14.32 ? 283 GLU A O   1 
ATOM   1722 C  CB  . GLU A 1 283 ? -2.192  9.845   8.077   1.00 14.40 ? 283 GLU A CB  1 
ATOM   1723 C  CG  . GLU A 1 283 ? -3.591  10.445  7.918   1.00 15.74 ? 283 GLU A CG  1 
ATOM   1724 C  CD  . GLU A 1 283 ? -3.659  11.939  8.036   1.00 15.13 ? 283 GLU A CD  1 
ATOM   1725 O  OE1 . GLU A 1 283 ? -2.657  12.529  8.518   1.00 14.76 ? 283 GLU A OE1 1 
ATOM   1726 O  OE2 . GLU A 1 283 ? -4.739  12.510  7.633   1.00 14.74 ? 283 GLU A OE2 1 
ATOM   1727 N  N   . THR A 1 284 ? -1.867  8.307   5.374   1.00 15.31 ? 284 THR A N   1 
ATOM   1728 C  CA  . THR A 1 284 ? -2.178  8.201   3.937   1.00 14.07 ? 284 THR A CA  1 
ATOM   1729 C  C   . THR A 1 284 ? -2.531  6.726   3.633   1.00 14.01 ? 284 THR A C   1 
ATOM   1730 O  O   . THR A 1 284 ? -3.501  6.402   2.952   1.00 14.45 ? 284 THR A O   1 
ATOM   1731 C  CB  . THR A 1 284 ? -0.996  8.774   3.155   1.00 14.69 ? 284 THR A CB  1 
ATOM   1732 O  OG1 . THR A 1 284 ? -0.513  9.998   3.792   1.00 18.54 ? 284 THR A OG1 1 
ATOM   1733 C  CG2 . THR A 1 284 ? -1.330  8.881   1.684   1.00 18.16 ? 284 THR A CG2 1 
ATOM   1734 N  N   . TRP A 1 285 ? -1.619  5.837   4.062   1.00 13.72 ? 285 TRP A N   1 
ATOM   1735 C  CA  . TRP A 1 285 ? -1.862  4.411   3.839   1.00 12.19 ? 285 TRP A CA  1 
ATOM   1736 C  C   . TRP A 1 285 ? -3.151  3.886   4.428   1.00 13.59 ? 285 TRP A C   1 
ATOM   1737 O  O   . TRP A 1 285 ? -3.843  3.063   3.777   1.00 15.83 ? 285 TRP A O   1 
ATOM   1738 C  CB  . TRP A 1 285 ? -0.676  3.658   4.414   1.00 12.24 ? 285 TRP A CB  1 
ATOM   1739 C  CG  . TRP A 1 285 ? -0.800  2.173   4.286   1.00 13.33 ? 285 TRP A CG  1 
ATOM   1740 C  CD1 . TRP A 1 285 ? -1.026  1.263   5.277   1.00 14.39 ? 285 TRP A CD1 1 
ATOM   1741 C  CD2 . TRP A 1 285 ? -0.451  1.411   3.127   1.00 14.09 ? 285 TRP A CD2 1 
ATOM   1742 N  NE1 . TRP A 1 285 ? -0.895  -0.004  4.810   1.00 13.30 ? 285 TRP A NE1 1 
ATOM   1743 C  CE2 . TRP A 1 285 ? -0.552  0.046   3.489   1.00 13.65 ? 285 TRP A CE2 1 
ATOM   1744 C  CE3 . TRP A 1 285 ? -0.096  1.735   1.820   1.00 15.99 ? 285 TRP A CE3 1 
ATOM   1745 C  CZ2 . TRP A 1 285 ? -0.330  -0.978  2.566   1.00 14.83 ? 285 TRP A CZ2 1 
ATOM   1746 C  CZ3 . TRP A 1 285 ? 0.101   0.720   0.923   1.00 17.27 ? 285 TRP A CZ3 1 
ATOM   1747 C  CH2 . TRP A 1 285 ? -0.035  -0.613  1.281   1.00 16.14 ? 285 TRP A CH2 1 
ATOM   1748 N  N   . ASP A 1 286 ? -3.489  4.261   5.675   1.00 13.50 ? 286 ASP A N   1 
ATOM   1749 C  CA  . ASP A 1 286 ? -4.580  3.648   6.413   1.00 15.16 ? 286 ASP A CA  1 
ATOM   1750 C  C   . ASP A 1 286 ? -5.930  4.088   5.820   1.00 15.04 ? 286 ASP A C   1 
ATOM   1751 O  O   . ASP A 1 286 ? -6.909  3.398   6.075   1.00 19.72 ? 286 ASP A O   1 
ATOM   1752 C  CB  . ASP A 1 286 ? -4.497  3.979   7.921   1.00 14.40 ? 286 ASP A CB  1 
ATOM   1753 C  CG  . ASP A 1 286 ? -3.401  3.221   8.652   1.00 14.29 ? 286 ASP A CG  1 
ATOM   1754 O  OD1 . ASP A 1 286 ? -2.858  2.283   8.060   1.00 13.83 ? 286 ASP A OD1 1 
ATOM   1755 O  OD2 . ASP A 1 286 ? -3.143  3.571   9.829   1.00 16.03 ? 286 ASP A OD2 1 
ATOM   1756 N  N   . ARG A 1 287 ? -5.949  5.139   4.985   1.00 15.07 ? 287 ARG A N   1 
ATOM   1757 C  CA  . ARG A 1 287 ? -7.190  5.523   4.326   1.00 14.35 ? 287 ARG A CA  1 
ATOM   1758 C  C   . ARG A 1 287 ? -7.286  4.921   2.928   1.00 18.57 ? 287 ARG A C   1 
ATOM   1759 O  O   . ARG A 1 287 ? -8.364  5.044   2.327   1.00 17.64 ? 287 ARG A O   1 
ATOM   1760 C  CB  . ARG A 1 287 ? -7.487  7.024   4.336   1.00 17.73 ? 287 ARG A CB  1 
ATOM   1761 C  CG  . ARG A 1 287 ? -6.526  7.847   3.501   1.00 18.88 ? 287 ARG A CG  1 
ATOM   1762 C  CD  . ARG A 1 287 ? -7.049  9.261   3.316   1.00 18.25 ? 287 ARG A CD  1 
ATOM   1763 N  NE  . ARG A 1 287 ? -6.115  10.060  2.513   1.00 15.46 ? 287 ARG A NE  1 
ATOM   1764 C  CZ  . ARG A 1 287 ? -5.038  10.693  2.949   1.00 16.81 ? 287 ARG A CZ  1 
ATOM   1765 N  NH1 . ARG A 1 287 ? -4.139  11.203  2.082   1.00 18.99 ? 287 ARG A NH1 1 
ATOM   1766 N  NH2 . ARG A 1 287 ? -4.867  10.800  4.258   1.00 18.38 ? 287 ARG A NH2 1 
ATOM   1767 N  N   . ALA A 1 288 ? -6.236  4.219   2.463   1.00 15.12 ? 288 ALA A N   1 
ATOM   1768 C  CA  . ALA A 1 288 ? -6.274  3.500   1.205   1.00 16.19 ? 288 ALA A CA  1 
ATOM   1769 C  C   . ALA A 1 288 ? -7.178  2.263   1.331   1.00 16.61 ? 288 ALA A C   1 
ATOM   1770 O  O   . ALA A 1 288 ? -7.262  1.575   2.378   1.00 15.24 ? 288 ALA A O   1 
ATOM   1771 C  CB  . ALA A 1 288 ? -4.891  3.140   0.752   1.00 15.30 ? 288 ALA A CB  1 
ATOM   1772 N  N   . SER A 1 289 ? -7.851  1.947   0.217   1.00 15.33 ? 289 SER A N   1 
ATOM   1773 C  CA  . SER A 1 289 ? -8.648  0.747   0.175   1.00 16.33 ? 289 SER A CA  1 
ATOM   1774 C  C   . SER A 1 289 ? -7.744  -0.492  0.198   1.00 13.29 ? 289 SER A C   1 
ATOM   1775 O  O   . SER A 1 289 ? -6.585  -0.437  -0.217  1.00 13.49 ? 289 SER A O   1 
ATOM   1776 C  CB  . SER A 1 289 ? -9.555  0.729   -1.058  1.00 17.29 ? 289 SER A CB  1 
ATOM   1777 O  OG  . SER A 1 289 ? -8.803  0.508   -2.231  1.00 18.36 ? 289 SER A OG  1 
ATOM   1778 N  N   . LEU A 1 290 ? -8.355  -1.603  0.581   1.00 14.11 ? 290 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 290 ? -7.694  -2.902  0.552   1.00 16.20 ? 290 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 290 ? -7.193  -3.216  -0.837  1.00 16.67 ? 290 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 290 ? -6.046  -3.591  -0.989  1.00 15.97 ? 290 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 290 ? -8.664  -3.972  1.070   1.00 18.42 ? 290 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 290 ? -8.099  -5.378  1.007   1.00 19.30 ? 290 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 290 ? -6.916  -5.524  1.954   1.00 19.84 ? 290 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 290 ? -9.176  -6.418  1.332   1.00 21.00 ? 290 LEU A CD2 1 
ATOM   1786 N  N   . GLN A 1 291 ? -8.007  -2.942  -1.882  1.00 13.99 ? 291 GLN A N   1 
ATOM   1787 C  CA  . GLN A 1 291 ? -7.547  -3.193  -3.242  1.00 18.27 ? 291 GLN A CA  1 
ATOM   1788 C  C   . GLN A 1 291 ? -6.323  -2.333  -3.585  1.00 15.28 ? 291 GLN A C   1 
ATOM   1789 O  O   . GLN A 1 291 ? -5.392  -2.836  -4.230  1.00 17.88 ? 291 GLN A O   1 
ATOM   1790 C  CB  . GLN A 1 291 ? -8.660  -2.942  -4.274  1.00 20.97 ? 291 GLN A CB  1 
ATOM   1791 C  CG  . GLN A 1 291 ? -8.277  -3.499  -5.655  1.00 29.36 ? 291 GLN A CG  1 
ATOM   1792 C  CD  . GLN A 1 291 ? -7.933  -4.986  -5.704  1.00 35.48 ? 291 GLN A CD  1 
ATOM   1793 O  OE1 . GLN A 1 291 ? -8.762  -5.857  -5.443  1.00 40.91 ? 291 GLN A OE1 1 
ATOM   1794 N  NE2 . GLN A 1 291 ? -6.691  -5.336  -6.033  1.00 32.08 ? 291 GLN A NE2 1 
ATOM   1795 N  N   . GLU A 1 292 ? -6.326  -1.045  -3.188  1.00 15.80 ? 292 GLU A N   1 
ATOM   1796 C  CA  . GLU A 1 292 ? -5.219  -0.162  -3.481  1.00 17.22 ? 292 GLU A CA  1 
ATOM   1797 C  C   . GLU A 1 292 ? -3.955  -0.719  -2.819  1.00 15.26 ? 292 GLU A C   1 
ATOM   1798 O  O   . GLU A 1 292 ? -2.910  -0.720  -3.451  1.00 14.35 ? 292 GLU A O   1 
ATOM   1799 C  CB  . GLU A 1 292 ? -5.481  1.275   -3.002  1.00 18.45 ? 292 GLU A CB  1 
ATOM   1800 C  CG  . GLU A 1 292 ? -6.417  2.061   -3.950  1.00 27.12 ? 292 GLU A CG  1 
ATOM   1801 C  CD  . GLU A 1 292 ? -6.903  3.420   -3.428  1.00 32.92 ? 292 GLU A CD  1 
ATOM   1802 O  OE1 . GLU A 1 292 ? -7.478  3.516   -2.286  1.00 24.96 ? 292 GLU A OE1 1 
ATOM   1803 N  N   . GLN A 1 293 ? -4.072  -1.139  -1.539  1.00 14.12 ? 293 GLN A N   1 
ATOM   1804 C  CA  . GLN A 1 293 ? -2.937  -1.682  -0.803  1.00 13.24 ? 293 GLN A CA  1 
ATOM   1805 C  C   . GLN A 1 293 ? -2.325  -2.921  -1.459  1.00 13.39 ? 293 GLN A C   1 
ATOM   1806 O  O   . GLN A 1 293 ? -1.109  -2.981  -1.691  1.00 13.00 ? 293 GLN A O   1 
ATOM   1807 C  CB  . GLN A 1 293 ? -3.312  -1.993  0.635   1.00 12.74 ? 293 GLN A CB  1 
ATOM   1808 C  CG  . GLN A 1 293 ? -3.693  -0.745  1.473   1.00 12.62 ? 293 GLN A CG  1 
ATOM   1809 C  CD  . GLN A 1 293 ? -3.827  -1.033  2.939   1.00 14.16 ? 293 GLN A CD  1 
ATOM   1810 O  OE1 . GLN A 1 293 ? -3.695  -2.174  3.383   1.00 13.93 ? 293 GLN A OE1 1 
ATOM   1811 N  NE2 . GLN A 1 293 ? -4.071  0.005   3.747   1.00 15.84 ? 293 GLN A NE2 1 
ATOM   1812 N  N   . GLU A 1 294 ? -3.179  -3.842  -1.862  1.00 13.83 ? 294 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 294 ? -2.724  -5.036  -2.526  1.00 13.47 ? 294 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 294 ? -2.148  -4.732  -3.897  1.00 14.60 ? 294 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 294 ? -1.169  -5.366  -4.277  1.00 15.22 ? 294 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 294 ? -3.846  -6.084  -2.547  1.00 13.45 ? 294 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 294 ? -4.283  -6.532  -1.182  1.00 13.80 ? 294 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 294 ? -5.310  -7.650  -1.198  1.00 17.40 ? 294 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 294 ? -5.940  -7.786  -2.255  1.00 18.33 ? 294 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 294 ? -5.439  -8.387  -0.167  1.00 15.33 ? 294 GLU A OE2 1 
ATOM   1821 N  N   . ASP A 1 295 ? -2.751  -3.802  -4.661  1.00 13.63 ? 295 ASP A N   1 
ATOM   1822 C  CA  . ASP A 1 295 ? -2.198  -3.451  -5.941  1.00 14.34 ? 295 ASP A CA  1 
ATOM   1823 C  C   . ASP A 1 295 ? -0.824  -2.798  -5.833  1.00 12.82 ? 295 ASP A C   1 
ATOM   1824 O  O   . ASP A 1 295 ? 0.006   -2.869  -6.740  1.00 13.56 ? 295 ASP A O   1 
ATOM   1825 C  CB  . ASP A 1 295 ? -3.098  -2.459  -6.667  1.00 17.86 ? 295 ASP A CB  1 
ATOM   1826 C  CG  . ASP A 1 295 ? -4.353  -3.036  -7.309  1.00 19.68 ? 295 ASP A CG  1 
ATOM   1827 O  OD1 . ASP A 1 295 ? -4.480  -4.217  -7.323  1.00 18.75 ? 295 ASP A OD1 1 
ATOM   1828 O  OD2 . ASP A 1 295 ? -5.215  -2.213  -7.680  1.00 23.16 ? 295 ASP A OD2 1 
ATOM   1829 N  N   . VAL A 1 296 ? -0.572  -2.067  -4.739  1.00 14.94 ? 296 VAL A N   1 
ATOM   1830 C  CA  . VAL A 1 296 ? 0.721   -1.437  -4.519  1.00 14.76 ? 296 VAL A CA  1 
ATOM   1831 C  C   . VAL A 1 296 ? 1.817   -2.479  -4.494  1.00 15.58 ? 296 VAL A C   1 
ATOM   1832 O  O   . VAL A 1 296 ? 2.898   -2.207  -5.017  1.00 17.72 ? 296 VAL A O   1 
ATOM   1833 C  CB  . VAL A 1 296 ? 0.781   -0.601  -3.221  1.00 15.01 ? 296 VAL A CB  1 
ATOM   1834 C  CG1 . VAL A 1 296 ? 2.214   -0.354  -2.806  1.00 16.08 ? 296 VAL A CG1 1 
ATOM   1835 C  CG2 . VAL A 1 296 ? -0.023  0.653   -3.383  1.00 15.32 ? 296 VAL A CG2 1 
ATOM   1836 N  N   . PHE A 1 297 ? 1.544   -3.638  -3.865  1.00 14.75 ? 297 PHE A N   1 
ATOM   1837 C  CA  . PHE A 1 297 ? 2.583   -4.634  -3.678  1.00 15.67 ? 297 PHE A CA  1 
ATOM   1838 C  C   . PHE A 1 297 ? 2.552   -5.729  -4.767  1.00 14.39 ? 297 PHE A C   1 
ATOM   1839 O  O   . PHE A 1 297 ? 3.604   -6.217  -5.133  1.00 15.44 ? 297 PHE A O   1 
ATOM   1840 C  CB  . PHE A 1 297 ? 2.480   -5.284  -2.291  1.00 14.63 ? 297 PHE A CB  1 
ATOM   1841 C  CG  . PHE A 1 297 ? 3.044   -4.381  -1.221  1.00 12.66 ? 297 PHE A CG  1 
ATOM   1842 C  CD1 . PHE A 1 297 ? 4.404   -4.060  -1.219  1.00 13.98 ? 297 PHE A CD1 1 
ATOM   1843 C  CD2 . PHE A 1 297 ? 2.221   -3.857  -0.252  1.00 13.58 ? 297 PHE A CD2 1 
ATOM   1844 C  CE1 . PHE A 1 297 ? 4.903   -3.144  -0.327  1.00 14.34 ? 297 PHE A CE1 1 
ATOM   1845 C  CE2 . PHE A 1 297 ? 2.736   -2.942  0.676   1.00 13.99 ? 297 PHE A CE2 1 
ATOM   1846 C  CZ  . PHE A 1 297 ? 4.077   -2.614  0.628   1.00 12.37 ? 297 PHE A CZ  1 
ATOM   1847 N  N   . GLY A 1 298 ? 1.372   -6.145  -5.185  1.00 12.74 ? 298 GLY A N   1 
ATOM   1848 C  CA  . GLY A 1 298 ? 1.241   -7.281  -6.083  1.00 13.80 ? 298 GLY A CA  1 
ATOM   1849 C  C   . GLY A 1 298 ? 1.051   -8.614  -5.358  1.00 15.16 ? 298 GLY A C   1 
ATOM   1850 O  O   . GLY A 1 298 ? 1.121   -9.696  -5.963  1.00 15.21 ? 298 GLY A O   1 
ATOM   1851 N  N   . ARG A 1 299 ? 0.855   -8.553  -4.016  1.00 13.85 ? 299 ARG A N   1 
ATOM   1852 C  CA  . ARG A 1 299 ? 0.509   -9.713  -3.224  1.00 15.21 ? 299 ARG A CA  1 
ATOM   1853 C  C   . ARG A 1 299 ? -0.722  -9.346  -2.408  1.00 14.12 ? 299 ARG A C   1 
ATOM   1854 O  O   . ARG A 1 299 ? -0.979  -8.165  -2.152  1.00 14.48 ? 299 ARG A O   1 
ATOM   1855 C  CB  . ARG A 1 299 ? 1.646   -10.085 -2.271  1.00 13.52 ? 299 ARG A CB  1 
ATOM   1856 C  CG  . ARG A 1 299 ? 2.882   -10.637 -2.965  1.00 14.06 ? 299 ARG A CG  1 
ATOM   1857 C  CD  . ARG A 1 299 ? 3.954   -10.966 -2.000  1.00 12.76 ? 299 ARG A CD  1 
ATOM   1858 N  NE  . ARG A 1 299 ? 5.099   -11.616 -2.608  1.00 14.72 ? 299 ARG A NE  1 
ATOM   1859 C  CZ  . ARG A 1 299 ? 5.261   -12.949 -2.706  1.00 14.03 ? 299 ARG A CZ  1 
ATOM   1860 N  NH1 . ARG A 1 299 ? 4.369   -13.849 -2.252  1.00 13.09 ? 299 ARG A NH1 1 
ATOM   1861 N  NH2 . ARG A 1 299 ? 6.433   -13.364 -3.184  1.00 14.52 ? 299 ARG A NH2 1 
ATOM   1862 N  N   . ASP A 1 300 ? -1.490  -10.329 -2.022  1.00 13.99 ? 300 ASP A N   1 
ATOM   1863 C  CA  . ASP A 1 300 ? -2.652  -10.123 -1.186  1.00 14.82 ? 300 ASP A CA  1 
ATOM   1864 C  C   . ASP A 1 300 ? -2.161  -9.944  0.262   1.00 15.47 ? 300 ASP A C   1 
ATOM   1865 O  O   . ASP A 1 300 ? -1.030  -10.314 0.627   1.00 15.54 ? 300 ASP A O   1 
ATOM   1866 C  CB  . ASP A 1 300 ? -3.723  -11.216 -1.334  1.00 19.31 ? 300 ASP A CB  1 
ATOM   1867 C  CG  . ASP A 1 300 ? -3.318  -12.475 -0.555  1.00 22.00 ? 300 ASP A CG  1 
ATOM   1868 O  OD1 . ASP A 1 300 ? -2.495  -13.143 -1.028  1.00 26.31 ? 300 ASP A OD1 1 
ATOM   1869 O  OD2 . ASP A 1 300 ? -3.750  -12.715 0.564   1.00 26.04 ? 300 ASP A OD2 1 
ATOM   1870 N  N   . LYS A 1 301 ? -3.016  -9.287  1.062   1.00 15.26 ? 301 LYS A N   1 
ATOM   1871 C  CA  . LYS A 1 301 ? -2.572  -8.840  2.385   1.00 15.68 ? 301 LYS A CA  1 
ATOM   1872 C  C   . LYS A 1 301 ? -2.627  -10.030 3.352   1.00 15.56 ? 301 LYS A C   1 
ATOM   1873 O  O   . LYS A 1 301 ? -1.724  -10.182 4.206   1.00 17.67 ? 301 LYS A O   1 
ATOM   1874 C  CB  . LYS A 1 301 ? -3.423  -7.640  2.847   1.00 15.99 ? 301 LYS A CB  1 
ATOM   1875 C  CG  . LYS A 1 301 ? -2.802  -6.939  4.041   1.00 15.78 ? 301 LYS A CG  1 
ATOM   1876 C  CD  . LYS A 1 301 ? -3.422  -5.620  4.295   1.00 14.40 ? 301 LYS A CD  1 
ATOM   1877 C  CE  . LYS A 1 301 ? -2.595  -4.917  5.362   1.00 14.95 ? 301 LYS A CE  1 
ATOM   1878 N  NZ  . LYS A 1 301 ? -3.122  -3.583  5.678   1.00 14.43 ? 301 LYS A NZ  1 
ATOM   1879 N  N   . GLY A 1 302 ? -3.725  -10.819 3.275   1.00 15.55 ? 302 GLY A N   1 
ATOM   1880 C  CA  . GLY A 1 302 ? -3.968  -11.885 4.271   1.00 15.73 ? 302 GLY A CA  1 
ATOM   1881 C  C   . GLY A 1 302 ? -2.918  -13.001 4.233   1.00 17.42 ? 302 GLY A C   1 
ATOM   1882 O  O   . GLY A 1 302 ? -2.207  -13.339 5.201   1.00 18.58 ? 302 GLY A O   1 
ATOM   1883 N  N   . GLU A 1 303 ? -2.796  -13.611 3.052   1.00 17.13 ? 303 GLU A N   1 
ATOM   1884 C  CA  . GLU A 1 303 ? -1.888  -14.745 2.874   1.00 17.44 ? 303 GLU A CA  1 
ATOM   1885 C  C   . GLU A 1 303 ? -0.503  -14.264 2.430   1.00 13.88 ? 303 GLU A C   1 
ATOM   1886 O  O   . GLU A 1 303 ? 0.521   -14.888 2.678   1.00 13.94 ? 303 GLU A O   1 
ATOM   1887 C  CB  . GLU A 1 303 ? -2.527  -15.690 1.847   1.00 18.14 ? 303 GLU A CB  1 
ATOM   1888 C  CG  . GLU A 1 303 ? -1.678  -16.868 1.347   1.00 17.09 ? 303 GLU A CG  1 
ATOM   1889 C  CD  . GLU A 1 303 ? -1.161  -17.817 2.430   1.00 19.39 ? 303 GLU A CD  1 
ATOM   1890 O  OE1 . GLU A 1 303 ? -1.885  -17.919 3.508   1.00 22.58 ? 303 GLU A OE1 1 
ATOM   1891 O  OE2 . GLU A 1 303 ? -0.125  -18.539 2.252   1.00 18.80 ? 303 GLU A OE2 1 
ATOM   1892 N  N   . GLY A 1 304 ? -0.466  -13.134 1.710   1.00 14.49 ? 304 GLY A N   1 
ATOM   1893 C  CA  . GLY A 1 304 ? 0.746   -12.648 1.123   1.00 12.88 ? 304 GLY A CA  1 
ATOM   1894 C  C   . GLY A 1 304 ? 1.134   -13.464 -0.109  1.00 13.80 ? 304 GLY A C   1 
ATOM   1895 O  O   . GLY A 1 304 ? 2.303   -13.511 -0.500  1.00 14.32 ? 304 GLY A O   1 
ATOM   1896 N  N   . ALA A 1 305 ? 0.132   -14.058 -0.778  1.00 12.44 ? 305 ALA A N   1 
ATOM   1897 C  CA  . ALA A 1 305 ? 0.394   -14.735 -2.053  1.00 14.39 ? 305 ALA A CA  1 
ATOM   1898 C  C   . ALA A 1 305 ? 0.552   -13.728 -3.169  1.00 13.79 ? 305 ALA A C   1 
ATOM   1899 O  O   . ALA A 1 305 ? -0.133  -12.690 -3.146  1.00 14.12 ? 305 ALA A O   1 
ATOM   1900 C  CB  . ALA A 1 305 ? -0.779  -15.636 -2.377  1.00 15.03 ? 305 ALA A CB  1 
ATOM   1901 N  N   . PRO A 1 306 ? 1.323   -14.049 -4.228  1.00 15.25 ? 306 PRO A N   1 
ATOM   1902 C  CA  . PRO A 1 306 ? 1.293   -13.243 -5.443  1.00 15.71 ? 306 PRO A CA  1 
ATOM   1903 C  C   . PRO A 1 306 ? -0.127  -13.219 -5.961  1.00 15.06 ? 306 PRO A C   1 
ATOM   1904 O  O   . PRO A 1 306 ? -0.893  -14.163 -5.757  1.00 16.93 ? 306 PRO A O   1 
ATOM   1905 C  CB  . PRO A 1 306 ? 2.223   -13.995 -6.418  1.00 16.90 ? 306 PRO A CB  1 
ATOM   1906 C  CG  . PRO A 1 306 ? 3.027   -14.957 -5.586  1.00 18.50 ? 306 PRO A CG  1 
ATOM   1907 C  CD  . PRO A 1 306 ? 2.157   -15.260 -4.379  1.00 16.25 ? 306 PRO A CD  1 
ATOM   1908 N  N   . VAL A 1 307 ? -0.479  -12.091 -6.581  1.00 16.30 ? 307 VAL A N   1 
ATOM   1909 C  CA  . VAL A 1 307 ? -1.809  -11.873 -7.105  1.00 19.56 ? 307 VAL A CA  1 
ATOM   1910 C  C   . VAL A 1 307 ? -2.235  -13.094 -7.915  1.00 18.65 ? 307 VAL A C   1 
ATOM   1911 O  O   . VAL A 1 307 ? -1.499  -13.575 -8.751  1.00 18.24 ? 307 VAL A O   1 
ATOM   1912 C  CB  . VAL A 1 307 ? -1.944  -10.522 -7.868  1.00 24.51 ? 307 VAL A CB  1 
ATOM   1913 C  CG1 . VAL A 1 307 ? -1.070  -10.425 -9.095  1.00 26.01 ? 307 VAL A CG1 1 
ATOM   1914 C  CG2 . VAL A 1 307 ? -3.411  -10.269 -8.196  1.00 27.20 ? 307 VAL A CG2 1 
ATOM   1915 N  N   . GLY A 1 308 ? -3.456  -13.560 -7.656  1.00 17.34 ? 308 GLY A N   1 
ATOM   1916 C  CA  . GLY A 1 308 ? -3.983  -14.678 -8.441  1.00 22.36 ? 308 GLY A CA  1 
ATOM   1917 C  C   . GLY A 1 308 ? -3.611  -16.052 -7.900  1.00 21.16 ? 308 GLY A C   1 
ATOM   1918 O  O   . GLY A 1 308 ? -4.291  -17.030 -8.231  1.00 23.79 ? 308 GLY A O   1 
ATOM   1919 N  N   . LYS A 1 309 ? -2.618  -16.167 -7.003  1.00 16.66 ? 309 LYS A N   1 
ATOM   1920 C  CA  . LYS A 1 309 ? -2.221  -17.444 -6.514  1.00 15.97 ? 309 LYS A CA  1 
ATOM   1921 C  C   . LYS A 1 309 ? -2.739  -17.593 -5.093  1.00 17.09 ? 309 LYS A C   1 
ATOM   1922 O  O   . LYS A 1 309 ? -3.230  -16.658 -4.480  1.00 18.87 ? 309 LYS A O   1 
ATOM   1923 C  CB  . LYS A 1 309 ? -0.715  -17.611 -6.666  1.00 13.87 ? 309 LYS A CB  1 
ATOM   1924 C  CG  . LYS A 1 309 ? -0.294  -17.734 -8.115  1.00 16.70 ? 309 LYS A CG  1 
ATOM   1925 C  CD  . LYS A 1 309 ? 1.137   -18.066 -8.284  1.00 16.14 ? 309 LYS A CD  1 
ATOM   1926 C  CE  . LYS A 1 309 ? 1.502   -18.546 -9.652  1.00 17.27 ? 309 LYS A CE  1 
ATOM   1927 N  NZ  . LYS A 1 309 ? 2.857   -19.061 -9.771  1.00 15.65 ? 309 LYS A NZ  1 
ATOM   1928 N  N   . ALA A 1 310 ? -2.555  -18.749 -4.526  1.00 17.22 ? 310 ALA A N   1 
ATOM   1929 C  CA  . ALA A 1 310 ? -3.238  -19.081 -3.284  1.00 19.66 ? 310 ALA A CA  1 
ATOM   1930 C  C   . ALA A 1 310 ? -2.280  -19.002 -2.079  1.00 17.82 ? 310 ALA A C   1 
ATOM   1931 O  O   . ALA A 1 310 ? -2.773  -18.833 -0.977  1.00 17.11 ? 310 ALA A O   1 
ATOM   1932 C  CB  . ALA A 1 310 ? -3.821  -20.481 -3.406  1.00 24.82 ? 310 ALA A CB  1 
ATOM   1933 N  N   . LYS A 1 311 ? -0.968  -19.281 -2.235  1.00 15.99 ? 311 LYS A N   1 
ATOM   1934 C  CA  . LYS A 1 311 ? -0.076  -19.434 -1.109  1.00 17.50 ? 311 LYS A CA  1 
ATOM   1935 C  C   . LYS A 1 311 ? 1.091   -18.441 -1.189  1.00 16.38 ? 311 LYS A C   1 
ATOM   1936 O  O   . LYS A 1 311 ? 1.552   -18.097 -2.263  1.00 15.41 ? 311 LYS A O   1 
ATOM   1937 C  CB  . LYS A 1 311 ? 0.446   -20.861 -1.095  1.00 21.65 ? 311 LYS A CB  1 
ATOM   1938 C  CG  . LYS A 1 311 ? -0.711  -21.878 -1.070  1.00 24.57 ? 311 LYS A CG  1 
ATOM   1939 C  CD  . LYS A 1 311 ? -1.399  -21.787 0.249   1.00 31.02 ? 311 LYS A CD  1 
ATOM   1940 C  CE  . LYS A 1 311 ? -2.787  -22.399 0.232   1.00 36.30 ? 311 LYS A CE  1 
ATOM   1941 N  NZ  . LYS A 1 311 ? -3.100  -22.761 1.618   1.00 33.48 ? 311 LYS A NZ  1 
ATOM   1942 N  N   . GLU A 1 312 ? 1.506   -18.006 -0.008  1.00 15.15 ? 312 GLU A N   1 
ATOM   1943 C  CA  . GLU A 1 312 ? 2.606   -17.076 0.163   1.00 13.43 ? 312 GLU A CA  1 
ATOM   1944 C  C   . GLU A 1 312 ? 3.795   -17.414 -0.732  1.00 13.87 ? 312 GLU A C   1 
ATOM   1945 O  O   . GLU A 1 312 ? 4.341   -16.485 -1.375  1.00 15.37 ? 312 GLU A O   1 
ATOM   1946 C  CB  . GLU A 1 312 ? 3.011   -17.076 1.619   1.00 14.53 ? 312 GLU A CB  1 
ATOM   1947 C  CG  . GLU A 1 312 ? 4.105   -16.038 1.906   1.00 13.52 ? 312 GLU A CG  1 
ATOM   1948 C  CD  . GLU A 1 312 ? 4.745   -16.089 3.274   1.00 14.72 ? 312 GLU A CD  1 
ATOM   1949 O  OE1 . GLU A 1 312 ? 4.169   -16.703 4.218   1.00 13.83 ? 312 GLU A OE1 1 
ATOM   1950 O  OE2 . GLU A 1 312 ? 5.818   -15.490 3.413   1.00 15.01 ? 312 GLU A OE2 1 
ATOM   1951 N  N   . ARG A 1 313 ? 4.210   -18.678 -0.692  1.00 13.90 ? 313 ARG A N   1 
ATOM   1952 C  CA  . ARG A 1 313 ? 5.459   -19.084 -1.313  1.00 16.18 ? 313 ARG A CA  1 
ATOM   1953 C  C   . ARG A 1 313 ? 5.286   -19.567 -2.753  1.00 13.97 ? 313 ARG A C   1 
ATOM   1954 O  O   . ARG A 1 313 ? 6.287   -19.975 -3.374  1.00 13.65 ? 313 ARG A O   1 
ATOM   1955 C  CB  . ARG A 1 313 ? 6.269   -20.048 -0.449  1.00 15.35 ? 313 ARG A CB  1 
ATOM   1956 C  CG  . ARG A 1 313 ? 6.739   -19.404 0.847   1.00 20.34 ? 313 ARG A CG  1 
ATOM   1957 C  CD  . ARG A 1 313 ? 7.682   -20.258 1.688   1.00 21.99 ? 313 ARG A CD  1 
ATOM   1958 N  NE  . ARG A 1 313 ? 8.160   -19.430 2.822   1.00 23.62 ? 313 ARG A NE  1 
ATOM   1959 C  CZ  . ARG A 1 313 ? 8.989   -18.355 2.686   1.00 22.23 ? 313 ARG A CZ  1 
ATOM   1960 N  NH1 . ARG A 1 313 ? 9.587   -18.090 1.538   1.00 19.06 ? 313 ARG A NH1 1 
ATOM   1961 N  NH2 . ARG A 1 313 ? 9.212   -17.570 3.720   1.00 26.43 ? 313 ARG A NH2 1 
ATOM   1962 N  N   . ASP A 1 314 ? 4.074   -19.490 -3.287  1.00 13.27 ? 314 ASP A N   1 
ATOM   1963 C  CA  . ASP A 1 314 ? 3.934   -19.700 -4.712  1.00 14.49 ? 314 ASP A CA  1 
ATOM   1964 C  C   . ASP A 1 314 ? 4.723   -18.624 -5.470  1.00 17.20 ? 314 ASP A C   1 
ATOM   1965 O  O   . ASP A 1 314 ? 4.846   -17.467 -4.995  1.00 15.36 ? 314 ASP A O   1 
ATOM   1966 C  CB  . ASP A 1 314 ? 2.494   -19.697 -5.155  1.00 17.33 ? 314 ASP A CB  1 
ATOM   1967 C  CG  . ASP A 1 314 ? 1.652   -20.854 -4.632  1.00 18.29 ? 314 ASP A CG  1 
ATOM   1968 O  OD1 . ASP A 1 314 ? 2.266   -21.897 -4.353  1.00 18.74 ? 314 ASP A OD1 1 
ATOM   1969 O  OD2 . ASP A 1 314 ? 0.374   -20.690 -4.654  1.00 19.76 ? 314 ASP A OD2 1 
ATOM   1970 N  N   . GLU A 1 315 ? 5.228   -18.972 -6.663  1.00 14.22 ? 315 GLU A N   1 
ATOM   1971 C  CA  . GLU A 1 315 ? 6.147   -18.037 -7.325  1.00 15.24 ? 315 GLU A CA  1 
ATOM   1972 C  C   . GLU A 1 315 ? 5.325   -16.926 -7.948  1.00 15.45 ? 315 GLU A C   1 
ATOM   1973 O  O   . GLU A 1 315 ? 4.308   -17.163 -8.581  1.00 15.37 ? 315 GLU A O   1 
ATOM   1974 C  CB  . GLU A 1 315 ? 6.951   -18.698 -8.436  1.00 19.76 ? 315 GLU A CB  1 
ATOM   1975 C  CG  . GLU A 1 315 ? 8.078   -19.574 -7.869  1.00 25.66 ? 315 GLU A CG  1 
ATOM   1976 C  CD  . GLU A 1 315 ? 9.117   -18.880 -7.011  1.00 26.12 ? 315 GLU A CD  1 
ATOM   1977 O  OE1 . GLU A 1 315 ? 9.313   -17.651 -7.145  1.00 34.69 ? 315 GLU A OE1 1 
ATOM   1978 O  OE2 . GLU A 1 315 ? 9.566   -19.517 -6.062  1.00 35.68 ? 315 GLU A OE2 1 
ATOM   1979 N  N   . PRO A 1 316 ? 5.794   -15.677 -7.904  1.00 15.45 ? 316 PRO A N   1 
ATOM   1980 C  CA  . PRO A 1 316 ? 5.057   -14.590 -8.540  1.00 16.93 ? 316 PRO A CA  1 
ATOM   1981 C  C   . PRO A 1 316 ? 4.971   -14.808 -10.044 1.00 14.63 ? 316 PRO A C   1 
ATOM   1982 O  O   . PRO A 1 316 ? 5.938   -15.294 -10.676 1.00 16.30 ? 316 PRO A O   1 
ATOM   1983 C  CB  . PRO A 1 316 ? 5.855   -13.346 -8.220  1.00 15.88 ? 316 PRO A CB  1 
ATOM   1984 C  CG  . PRO A 1 316 ? 6.989   -13.735 -7.449  1.00 18.46 ? 316 PRO A CG  1 
ATOM   1985 C  CD  . PRO A 1 316 ? 6.956   -15.224 -7.143  1.00 17.19 ? 316 PRO A CD  1 
ATOM   1986 N  N   . PHE A 1 317 ? 3.798   -14.461 -10.569 1.00 14.19 ? 317 PHE A N   1 
ATOM   1987 C  CA  . PHE A 1 317 ? 3.618   -14.292 -11.997 1.00 15.29 ? 317 PHE A CA  1 
ATOM   1988 C  C   . PHE A 1 317 ? 3.513   -12.792 -12.286 1.00 16.50 ? 317 PHE A C   1 
ATOM   1989 O  O   . PHE A 1 317 ? 2.490   -12.152 -12.065 1.00 18.62 ? 317 PHE A O   1 
ATOM   1990 C  CB  . PHE A 1 317 ? 2.418   -15.136 -12.453 1.00 16.40 ? 317 PHE A CB  1 
ATOM   1991 C  CG  . PHE A 1 317 ? 2.226   -15.123 -13.938 1.00 18.67 ? 317 PHE A CG  1 
ATOM   1992 C  CD1 . PHE A 1 317 ? 3.080   -15.862 -14.737 1.00 25.64 ? 317 PHE A CD1 1 
ATOM   1993 C  CD2 . PHE A 1 317 ? 1.206   -14.382 -14.538 1.00 25.90 ? 317 PHE A CD2 1 
ATOM   1994 C  CE1 . PHE A 1 317 ? 2.890   -15.894 -16.112 1.00 29.00 ? 317 PHE A CE1 1 
ATOM   1995 C  CE2 . PHE A 1 317 ? 1.031   -14.419 -15.908 1.00 26.61 ? 317 PHE A CE2 1 
ATOM   1996 C  CZ  . PHE A 1 317 ? 1.855   -15.195 -16.680 1.00 29.88 ? 317 PHE A CZ  1 
ATOM   1997 N  N   . LEU A 1 318 ? 4.628   -12.204 -12.700 1.00 16.17 ? 318 LEU A N   1 
ATOM   1998 C  CA  . LEU A 1 318 ? 4.779   -10.763 -12.680 1.00 15.62 ? 318 LEU A CA  1 
ATOM   1999 C  C   . LEU A 1 318 ? 3.807   -10.086 -13.649 1.00 19.75 ? 318 LEU A C   1 
ATOM   2000 O  O   . LEU A 1 318 ? 3.354   -8.985  -13.326 1.00 17.49 ? 318 LEU A O   1 
ATOM   2001 C  CB  . LEU A 1 318 ? 6.221   -10.403 -13.026 1.00 18.92 ? 318 LEU A CB  1 
ATOM   2002 C  CG  . LEU A 1 318 ? 7.299   -10.807 -12.014 1.00 21.06 ? 318 LEU A CG  1 
ATOM   2003 C  CD1 . LEU A 1 318 ? 8.606   -10.076 -12.296 1.00 23.87 ? 318 LEU A CD1 1 
ATOM   2004 C  CD2 . LEU A 1 318 ? 6.910   -10.548 -10.584 1.00 21.05 ? 318 LEU A CD2 1 
ATOM   2005 N  N   . LYS A 1 319 ? 3.462   -10.721 -14.789 1.00 17.56 ? 319 LYS A N   1 
ATOM   2006 C  CA  . LYS A 1 319 ? 2.601   -10.011 -15.746 1.00 21.69 ? 319 LYS A CA  1 
ATOM   2007 C  C   . LYS A 1 319 ? 1.175   -9.810  -15.226 1.00 22.32 ? 319 LYS A C   1 
ATOM   2008 O  O   . LYS A 1 319 ? 0.445   -8.978  -15.724 1.00 21.40 ? 319 LYS A O   1 
ATOM   2009 C  CB  . LYS A 1 319 ? 2.529   -10.756 -17.091 1.00 27.98 ? 319 LYS A CB  1 
ATOM   2010 C  CG  . LYS A 1 319 ? 3.735   -10.575 -18.015 1.00 33.76 ? 319 LYS A CG  1 
ATOM   2011 N  N   . ALA A 1 320 ? 0.774   -10.449 -14.136 1.00 19.99 ? 320 ALA A N   1 
ATOM   2012 C  CA  . ALA A 1 320 ? -0.542  -10.287 -13.558 1.00 19.81 ? 320 ALA A CA  1 
ATOM   2013 C  C   . ALA A 1 320 ? -0.557  -9.098  -12.580 1.00 17.55 ? 320 ALA A C   1 
ATOM   2014 O  O   . ALA A 1 320 ? -1.603  -8.668  -12.176 1.00 20.21 ? 320 ALA A O   1 
ATOM   2015 C  CB  . ALA A 1 320 ? -0.948  -11.568 -12.849 1.00 22.41 ? 320 ALA A CB  1 
ATOM   2016 N  N   . MET A 1 321 ? 0.614   -8.607  -12.196 1.00 15.98 ? 321 MET A N   1 
ATOM   2017 C  CA  . MET A 1 321 ? 0.722   -7.471  -11.297 1.00 16.75 ? 321 MET A CA  1 
ATOM   2018 C  C   . MET A 1 321 ? 0.637   -6.176  -12.119 1.00 17.39 ? 321 MET A C   1 
ATOM   2019 O  O   . MET A 1 321 ? 0.961   -6.128  -13.305 1.00 18.96 ? 321 MET A O   1 
ATOM   2020 C  CB  . MET A 1 321 ? 2.072   -7.525  -10.553 1.00 18.24 ? 321 MET A CB  1 
ATOM   2021 C  CG  . MET A 1 321 ? 2.187   -8.716  -9.660  1.00 15.83 ? 321 MET A CG  1 
ATOM   2022 S  SD  . MET A 1 321 ? 3.797   -8.737  -8.919  1.00 17.70 ? 321 MET A SD  1 
ATOM   2023 C  CE  . MET A 1 321 ? 3.640   -10.337 -8.141  1.00 18.40 ? 321 MET A CE  1 
ATOM   2024 N  N   . LYS A 1 322 ? 0.197   -5.095  -11.477 1.00 18.42 ? 322 LYS A N   1 
ATOM   2025 C  CA  . LYS A 1 322 ? 0.316   -3.764  -12.057 1.00 18.72 ? 322 LYS A CA  1 
ATOM   2026 C  C   . LYS A 1 322 ? 1.768   -3.481  -12.409 1.00 18.66 ? 322 LYS A C   1 
ATOM   2027 O  O   . LYS A 1 322 ? 2.700   -3.952  -11.762 1.00 17.36 ? 322 LYS A O   1 
ATOM   2028 C  CB  . LYS A 1 322 ? -0.273  -2.693  -11.114 1.00 23.60 ? 322 LYS A CB  1 
ATOM   2029 C  CG  . LYS A 1 322 ? -1.731  -2.904  -10.713 1.00 29.06 ? 322 LYS A CG  1 
ATOM   2030 C  CD  . LYS A 1 322 ? -2.754  -2.214  -11.547 1.00 33.41 ? 322 LYS A CD  1 
ATOM   2031 C  CE  . LYS A 1 322 ? -4.169  -2.542  -11.105 1.00 34.55 ? 322 LYS A CE  1 
ATOM   2032 N  N   . PRO A 1 323 ? 2.018   -2.671  -13.465 1.00 21.61 ? 323 PRO A N   1 
ATOM   2033 C  CA  . PRO A 1 323 ? 3.378   -2.363  -13.900 1.00 21.63 ? 323 PRO A CA  1 
ATOM   2034 C  C   . PRO A 1 323 ? 4.186   -1.560  -12.879 1.00 17.50 ? 323 PRO A C   1 
ATOM   2035 O  O   . PRO A 1 323 ? 5.398   -1.615  -12.926 1.00 21.72 ? 323 PRO A O   1 
ATOM   2036 C  CB  . PRO A 1 323 ? 3.227   -1.462  -15.147 1.00 27.39 ? 323 PRO A CB  1 
ATOM   2037 C  CG  . PRO A 1 323 ? 1.733   -1.373  -15.427 1.00 28.41 ? 323 PRO A CG  1 
ATOM   2038 C  CD  . PRO A 1 323 ? 0.973   -2.188  -14.419 1.00 25.67 ? 323 PRO A CD  1 
ATOM   2039 N  N   . ASP A 1 324 ? 3.503   -0.906  -11.949 1.00 16.13 ? 324 ASP A N   1 
ATOM   2040 C  CA  . ASP A 1 324 ? 4.208   -0.172  -10.884 1.00 17.43 ? 324 ASP A CA  1 
ATOM   2041 C  C   . ASP A 1 324 ? 4.168   -0.866  -9.519  1.00 15.61 ? 324 ASP A C   1 
ATOM   2042 O  O   . ASP A 1 324 ? 4.500   -0.257  -8.466  1.00 15.85 ? 324 ASP A O   1 
ATOM   2043 C  CB  . ASP A 1 324 ? 3.664   1.250   -10.768 1.00 18.94 ? 324 ASP A CB  1 
ATOM   2044 C  CG  . ASP A 1 324 ? 2.139   1.399   -10.479 1.00 22.93 ? 324 ASP A CG  1 
ATOM   2045 O  OD1 . ASP A 1 324 ? 1.335   0.388   -10.462 1.00 22.50 ? 324 ASP A OD1 1 
ATOM   2046 O  OD2 . ASP A 1 324 ? 1.702   2.559   -10.316 1.00 25.94 ? 324 ASP A OD2 1 
ATOM   2047 N  N   . ALA A 1 325 ? 3.744   -2.131  -9.509  1.00 16.09 ? 325 ALA A N   1 
ATOM   2048 C  CA  . ALA A 1 325 ? 3.698   -2.872  -8.276  1.00 15.32 ? 325 ALA A CA  1 
ATOM   2049 C  C   . ALA A 1 325 ? 5.132   -3.003  -7.743  1.00 14.36 ? 325 ALA A C   1 
ATOM   2050 O  O   . ALA A 1 325 ? 6.064   -3.369  -8.456  1.00 14.26 ? 325 ALA A O   1 
ATOM   2051 C  CB  . ALA A 1 325 ? 3.051   -4.214  -8.490  1.00 15.06 ? 325 ALA A CB  1 
ATOM   2052 N  N   . HIS A 1 326 ? 5.245   -2.932  -6.422  1.00 12.22 ? 326 HIS A N   1 
ATOM   2053 C  CA  . HIS A 1 326 ? 6.532   -3.043  -5.762  1.00 12.11 ? 326 HIS A CA  1 
ATOM   2054 C  C   . HIS A 1 326 ? 7.241   -4.363  -6.074  1.00 11.78 ? 326 HIS A C   1 
ATOM   2055 O  O   . HIS A 1 326 ? 8.426   -4.352  -6.385  1.00 13.92 ? 326 HIS A O   1 
ATOM   2056 C  CB  . HIS A 1 326 ? 6.341   -2.828  -4.258  1.00 13.13 ? 326 HIS A CB  1 
ATOM   2057 C  CG  . HIS A 1 326 ? 7.623   -2.866  -3.484  1.00 14.06 ? 326 HIS A CG  1 
ATOM   2058 N  ND1 . HIS A 1 326 ? 8.547   -1.825  -3.462  1.00 13.82 ? 326 HIS A ND1 1 
ATOM   2059 C  CD2 . HIS A 1 326 ? 8.103   -3.855  -2.672  1.00 13.35 ? 326 HIS A CD2 1 
ATOM   2060 C  CE1 . HIS A 1 326 ? 9.542   -2.177  -2.668  1.00 16.34 ? 326 HIS A CE1 1 
ATOM   2061 N  NE2 . HIS A 1 326 ? 9.279   -3.403  -2.149  1.00 13.36 ? 326 HIS A NE2 1 
ATOM   2062 N  N   . VAL A 1 327 ? 6.566   -5.479  -5.919  1.00 12.58 ? 327 VAL A N   1 
ATOM   2063 C  CA  . VAL A 1 327 ? 7.187   -6.775  -6.132  1.00 13.93 ? 327 VAL A CA  1 
ATOM   2064 C  C   . VAL A 1 327 ? 7.597   -6.914  -7.582  1.00 15.42 ? 327 VAL A C   1 
ATOM   2065 O  O   . VAL A 1 327 ? 8.706   -7.371  -7.850  1.00 14.17 ? 327 VAL A O   1 
ATOM   2066 C  CB  . VAL A 1 327 ? 6.271   -7.934  -5.745  1.00 13.82 ? 327 VAL A CB  1 
ATOM   2067 C  CG1 . VAL A 1 327 ? 6.801   -9.254  -6.229  1.00 16.27 ? 327 VAL A CG1 1 
ATOM   2068 C  CG2 . VAL A 1 327 ? 6.133   -7.922  -4.230  1.00 15.97 ? 327 VAL A CG2 1 
ATOM   2069 N  N   . ARG A 1 328 ? 6.746   -6.432  -8.515  1.00 15.78 ? 328 ARG A N   1 
ATOM   2070 C  CA  . ARG A 1 328 ? 7.167   -6.499  -9.906  1.00 17.00 ? 328 ARG A CA  1 
ATOM   2071 C  C   . ARG A 1 328 ? 8.459   -5.723  -10.180 1.00 16.30 ? 328 ARG A C   1 
ATOM   2072 O  O   . ARG A 1 328 ? 9.365   -6.197  -10.870 1.00 18.12 ? 328 ARG A O   1 
ATOM   2073 C  CB  . ARG A 1 328 ? 6.030   -6.005  -10.785 1.00 15.90 ? 328 ARG A CB  1 
ATOM   2074 C  CG  . ARG A 1 328 ? 6.278   -6.230  -12.268 1.00 16.80 ? 328 ARG A CG  1 
ATOM   2075 C  CD  . ARG A 1 328 ? 4.987   -6.023  -12.989 1.00 20.30 ? 328 ARG A CD  1 
ATOM   2076 N  NE  . ARG A 1 328 ? 5.267   -5.944  -14.416 1.00 26.06 ? 328 ARG A NE  1 
ATOM   2077 C  CZ  . ARG A 1 328 ? 4.330   -6.034  -15.351 1.00 27.81 ? 328 ARG A CZ  1 
ATOM   2078 N  NH1 . ARG A 1 328 ? 3.071   -6.057  -15.017 1.00 23.65 ? 328 ARG A NH1 1 
ATOM   2079 N  NH2 . ARG A 1 328 ? 4.680   -6.131  -16.625 1.00 29.06 ? 328 ARG A NH2 1 
ATOM   2080 N  N   . LEU A 1 329 ? 8.550   -4.488  -9.640  1.00 15.62 ? 329 LEU A N   1 
ATOM   2081 C  CA  . LEU A 1 329 ? 9.718   -3.653  -9.863  1.00 14.83 ? 329 LEU A CA  1 
ATOM   2082 C  C   . LEU A 1 329 ? 10.971  -4.174  -9.150  1.00 16.83 ? 329 LEU A C   1 
ATOM   2083 O  O   . LEU A 1 329 ? 12.094  -3.944  -9.615  1.00 14.71 ? 329 LEU A O   1 
ATOM   2084 C  CB  . LEU A 1 329 ? 9.354   -2.242  -9.490  1.00 15.03 ? 329 LEU A CB  1 
ATOM   2085 C  CG  . LEU A 1 329 ? 8.324   -1.593  -10.401 1.00 17.84 ? 329 LEU A CG  1 
ATOM   2086 C  CD1 . LEU A 1 329 ? 8.005   -0.206  -9.889  1.00 19.05 ? 329 LEU A CD1 1 
ATOM   2087 C  CD2 . LEU A 1 329 ? 8.841   -1.544  -11.841 1.00 20.61 ? 329 LEU A CD2 1 
ATOM   2088 N  N   . ALA A 1 330 ? 10.821  -4.813  -7.985  1.00 12.33 ? 330 ALA A N   1 
ATOM   2089 C  CA  . ALA A 1 330 ? 11.995  -5.153  -7.177  1.00 13.84 ? 330 ALA A CA  1 
ATOM   2090 C  C   . ALA A 1 330 ? 12.529  -6.541  -7.481  1.00 13.21 ? 330 ALA A C   1 
ATOM   2091 O  O   . ALA A 1 330 ? 13.636  -6.862  -7.094  1.00 15.30 ? 330 ALA A O   1 
ATOM   2092 C  CB  . ALA A 1 330 ? 11.607  -5.104  -5.689  1.00 14.48 ? 330 ALA A CB  1 
ATOM   2093 N  N   . HIS A 1 331 ? 11.722  -7.353  -8.155  1.00 15.09 ? 331 HIS A N   1 
ATOM   2094 C  CA  . HIS A 1 331 ? 12.033  -8.758  -8.424  1.00 16.23 ? 331 HIS A CA  1 
ATOM   2095 C  C   . HIS A 1 331 ? 13.317  -8.895  -9.233  1.00 16.32 ? 331 HIS A C   1 
ATOM   2096 O  O   . HIS A 1 331 ? 13.588  -8.091  -10.110 1.00 16.24 ? 331 HIS A O   1 
ATOM   2097 C  CB  . HIS A 1 331 ? 10.887  -9.384  -9.221  1.00 15.99 ? 331 HIS A CB  1 
ATOM   2098 C  CG  . HIS A 1 331 ? 10.926  -10.894 -9.311  1.00 16.14 ? 331 HIS A CG  1 
ATOM   2099 N  ND1 . HIS A 1 331 ? 11.758  -11.608 -10.142 1.00 17.79 ? 331 HIS A ND1 1 
ATOM   2100 C  CD2 . HIS A 1 331 ? 10.183  -11.817 -8.675  1.00 17.08 ? 331 HIS A CD2 1 
ATOM   2101 C  CE1 . HIS A 1 331 ? 11.541  -12.914 -9.965  1.00 18.51 ? 331 HIS A CE1 1 
ATOM   2102 N  NE2 . HIS A 1 331 ? 10.548  -13.072 -9.092  1.00 18.16 ? 331 HIS A NE2 1 
ATOM   2103 N  N   . PRO A 1 332 ? 14.182  -9.869  -8.939  1.00 16.92 ? 332 PRO A N   1 
ATOM   2104 C  CA  . PRO A 1 332 ? 15.441  -10.020 -9.701  1.00 19.18 ? 332 PRO A CA  1 
ATOM   2105 C  C   . PRO A 1 332 ? 15.241  -10.085 -11.215 1.00 17.72 ? 332 PRO A C   1 
ATOM   2106 O  O   . PRO A 1 332 ? 16.078  -9.507  -11.921 1.00 20.56 ? 332 PRO A O   1 
ATOM   2107 C  CB  . PRO A 1 332 ? 15.951  -11.348 -9.124  1.00 21.04 ? 332 PRO A CB  1 
ATOM   2108 C  CG  . PRO A 1 332 ? 15.519  -11.343 -7.685  1.00 21.13 ? 332 PRO A CG  1 
ATOM   2109 C  CD  . PRO A 1 332 ? 14.116  -10.777 -7.779  1.00 18.35 ? 332 PRO A CD  1 
ATOM   2110 N  N   . ASP A 1 333 ? 14.131  -10.696 -11.681 1.00 17.66 ? 333 ASP A N   1 
ATOM   2111 C  CA  . ASP A 1 333 ? 13.871  -10.847 -13.110 1.00 20.06 ? 333 ASP A CA  1 
ATOM   2112 C  C   . ASP A 1 333 ? 13.655  -9.497  -13.792 1.00 21.23 ? 333 ASP A C   1 
ATOM   2113 O  O   . ASP A 1 333 ? 13.817  -9.407  -15.037 1.00 22.29 ? 333 ASP A O   1 
ATOM   2114 C  CB  . ASP A 1 333 ? 12.677  -11.757 -13.415 1.00 25.19 ? 333 ASP A CB  1 
ATOM   2115 C  CG  . ASP A 1 333 ? 12.864  -13.244 -13.188 1.00 28.51 ? 333 ASP A CG  1 
ATOM   2116 O  OD1 . ASP A 1 333 ? 13.962  -13.678 -12.772 1.00 32.27 ? 333 ASP A OD1 1 
ATOM   2117 O  OD2 . ASP A 1 333 ? 11.890  -13.955 -13.397 1.00 34.05 ? 333 ASP A OD2 1 
ATOM   2118 N  N   . SER A 1 334 ? 13.271  -8.460  -13.015 1.00 16.07 ? 334 SER A N   1 
ATOM   2119 C  CA  . SER A 1 334 ? 13.024  -7.109  -13.494 1.00 18.57 ? 334 SER A CA  1 
ATOM   2120 C  C   . SER A 1 334 ? 14.315  -6.306  -13.455 1.00 17.32 ? 334 SER A C   1 
ATOM   2121 O  O   . SER A 1 334 ? 14.356  -5.179  -13.925 1.00 20.76 ? 334 SER A O   1 
ATOM   2122 C  CB  . SER A 1 334 ? 11.883  -6.364  -12.786 1.00 18.19 ? 334 SER A CB  1 
ATOM   2123 O  OG  . SER A 1 334 ? 10.700  -7.123  -12.852 1.00 18.33 ? 334 SER A OG  1 
ATOM   2124 N  N   . ASN A 1 335 ? 15.409  -6.874  -12.895 1.00 17.76 ? 335 ASN A N   1 
ATOM   2125 C  CA  . ASN A 1 335 ? 16.602  -6.093  -12.562 1.00 17.12 ? 335 ASN A CA  1 
ATOM   2126 C  C   . ASN A 1 335 ? 17.861  -6.850  -13.005 1.00 19.00 ? 335 ASN A C   1 
ATOM   2127 O  O   . ASN A 1 335 ? 18.887  -6.759  -12.358 1.00 19.79 ? 335 ASN A O   1 
ATOM   2128 C  CB  . ASN A 1 335 ? 16.731  -5.777  -11.068 1.00 17.47 ? 335 ASN A CB  1 
ATOM   2129 C  CG  . ASN A 1 335 ? 15.680  -4.805  -10.644 1.00 18.96 ? 335 ASN A CG  1 
ATOM   2130 O  OD1 . ASN A 1 335 ? 15.801  -3.637  -10.963 1.00 20.71 ? 335 ASN A OD1 1 
ATOM   2131 N  ND2 . ASN A 1 335 ? 14.613  -5.305  -10.036 1.00 17.45 ? 335 ASN A ND2 1 
ATOM   2132 N  N   . GLY A 1 336 ? 17.770  -7.567  -14.132 1.00 18.94 ? 336 GLY A N   1 
ATOM   2133 C  CA  . GLY A 1 336 ? 18.929  -8.297  -14.647 1.00 23.58 ? 336 GLY A CA  1 
ATOM   2134 C  C   . GLY A 1 336 ? 19.500  -9.319  -13.682 1.00 24.14 ? 336 GLY A C   1 
ATOM   2135 O  O   . GLY A 1 336 ? 20.692  -9.666  -13.737 1.00 22.69 ? 336 GLY A O   1 
ATOM   2136 N  N   . GLY A 1 337 ? 18.641  -9.857  -12.786 1.00 20.54 ? 337 GLY A N   1 
ATOM   2137 C  CA  . GLY A 1 337 ? 19.083  -10.880 -11.865 1.00 22.91 ? 337 GLY A CA  1 
ATOM   2138 C  C   . GLY A 1 337 ? 19.531  -10.331 -10.504 1.00 18.47 ? 337 GLY A C   1 
ATOM   2139 O  O   . GLY A 1 337 ? 19.814  -11.145 -9.653  1.00 23.07 ? 337 GLY A O   1 
ATOM   2140 N  N   . ALA A 1 338 ? 19.565  -9.008  -10.307 1.00 18.94 ? 338 ALA A N   1 
ATOM   2141 C  CA  . ALA A 1 338 ? 20.073  -8.410  -9.078  1.00 18.40 ? 338 ALA A CA  1 
ATOM   2142 C  C   . ALA A 1 338 ? 19.234  -8.876  -7.872  1.00 18.11 ? 338 ALA A C   1 
ATOM   2143 O  O   . ALA A 1 338 ? 18.009  -8.776  -7.914  1.00 16.79 ? 338 ALA A O   1 
ATOM   2144 C  CB  . ALA A 1 338 ? 20.010  -6.942  -9.196  1.00 18.68 ? 338 ALA A CB  1 
ATOM   2145 N  N   . THR A 1 339 ? 19.928  -9.386  -6.844  1.00 19.30 ? 339 THR A N   1 
ATOM   2146 C  CA  . THR A 1 339 ? 19.271  -10.035 -5.729  1.00 17.84 ? 339 THR A CA  1 
ATOM   2147 C  C   . THR A 1 339 ? 19.973  -9.507  -4.472  1.00 16.74 ? 339 THR A C   1 
ATOM   2148 O  O   . THR A 1 339 ? 21.184  -9.305  -4.503  1.00 19.79 ? 339 THR A O   1 
ATOM   2149 C  CB  . THR A 1 339 ? 19.376  -11.553 -5.831  1.00 18.30 ? 339 THR A CB  1 
ATOM   2150 O  OG1 . THR A 1 339 ? 18.904  -11.988 -7.107  1.00 18.45 ? 339 THR A OG1 1 
ATOM   2151 C  CG2 . THR A 1 339 ? 18.601  -12.264 -4.734  1.00 18.26 ? 339 THR A CG2 1 
ATOM   2152 N  N   . LEU A 1 340 ? 19.200  -9.333  -3.399  1.00 16.16 ? 340 LEU A N   1 
ATOM   2153 C  CA  . LEU A 1 340 ? 19.633  -8.677  -2.179  1.00 17.69 ? 340 LEU A CA  1 
ATOM   2154 C  C   . LEU A 1 340 ? 19.290  -9.566  -1.000  1.00 12.72 ? 340 LEU A C   1 
ATOM   2155 O  O   . LEU A 1 340 ? 18.316  -10.291 -1.060  1.00 13.61 ? 340 LEU A O   1 
ATOM   2156 C  CB  . LEU A 1 340 ? 18.826  -7.387  -1.916  1.00 21.23 ? 340 LEU A CB  1 
ATOM   2157 C  CG  . LEU A 1 340 ? 18.901  -6.301  -2.948  1.00 22.24 ? 340 LEU A CG  1 
ATOM   2158 C  CD1 . LEU A 1 340 ? 18.019  -5.138  -2.526  1.00 28.92 ? 340 LEU A CD1 1 
ATOM   2159 C  CD2 . LEU A 1 340 ? 20.321  -5.844  -3.068  1.00 27.61 ? 340 LEU A CD2 1 
ATOM   2160 N  N   . LEU A 1 341 ? 20.096  -9.491  0.078   1.00 11.51 ? 341 LEU A N   1 
ATOM   2161 C  CA  . LEU A 1 341 ? 19.679  -10.020 1.373   1.00 12.42 ? 341 LEU A CA  1 
ATOM   2162 C  C   . LEU A 1 341 ? 19.100  -8.907  2.226   1.00 12.65 ? 341 LEU A C   1 
ATOM   2163 O  O   . LEU A 1 341 ? 19.828  -8.048  2.680   1.00 13.05 ? 341 LEU A O   1 
ATOM   2164 C  CB  . LEU A 1 341 ? 20.842  -10.746 2.074   1.00 12.43 ? 341 LEU A CB  1 
ATOM   2165 C  CG  . LEU A 1 341 ? 20.356  -11.639 3.214   1.00 14.45 ? 341 LEU A CG  1 
ATOM   2166 C  CD1 . LEU A 1 341 ? 21.322  -12.758 3.448   1.00 18.86 ? 341 LEU A CD1 1 
ATOM   2167 C  CD2 . LEU A 1 341 ? 20.203  -10.844 4.467   1.00 16.06 ? 341 LEU A CD2 1 
ATOM   2168 N  N   . ARG A 1 342 ? 17.756  -8.873  2.379   1.00 11.04 ? 342 ARG A N   1 
ATOM   2169 C  CA  . ARG A 1 342 ? 17.130  -7.883  3.199   1.00 10.87 ? 342 ARG A CA  1 
ATOM   2170 C  C   . ARG A 1 342 ? 17.063  -8.333  4.644   1.00 11.91 ? 342 ARG A C   1 
ATOM   2171 O  O   . ARG A 1 342 ? 16.731  -9.474  4.933   1.00 14.20 ? 342 ARG A O   1 
ATOM   2172 C  CB  . ARG A 1 342 ? 15.738  -7.630  2.651   1.00 11.69 ? 342 ARG A CB  1 
ATOM   2173 C  CG  . ARG A 1 342 ? 15.727  -7.007  1.272   1.00 12.66 ? 342 ARG A CG  1 
ATOM   2174 C  CD  . ARG A 1 342 ? 14.339  -6.908  0.732   1.00 13.39 ? 342 ARG A CD  1 
ATOM   2175 N  NE  . ARG A 1 342 ? 13.840  -8.211  0.332   1.00 13.53 ? 342 ARG A NE  1 
ATOM   2176 C  CZ  . ARG A 1 342 ? 12.634  -8.696  0.540   1.00 15.11 ? 342 ARG A CZ  1 
ATOM   2177 N  NH1 . ARG A 1 342 ? 11.707  -7.981  1.165   1.00 13.69 ? 342 ARG A NH1 1 
ATOM   2178 N  NH2 . ARG A 1 342 ? 12.418  -9.910  0.098   1.00 14.96 ? 342 ARG A NH2 1 
ATOM   2179 N  N   . ARG A 1 343 ? 17.345  -7.388  5.548   1.00 11.63 ? 343 ARG A N   1 
ATOM   2180 C  CA  . ARG A 1 343 ? 17.455  -7.720  6.969   1.00 11.95 ? 343 ARG A CA  1 
ATOM   2181 C  C   . ARG A 1 343 ? 16.982  -6.592  7.890   1.00 12.11 ? 343 ARG A C   1 
ATOM   2182 O  O   . ARG A 1 343 ? 17.548  -6.400  8.973   1.00 13.51 ? 343 ARG A O   1 
ATOM   2183 C  CB  . ARG A 1 343 ? 18.900  -8.132  7.273   1.00 11.73 ? 343 ARG A CB  1 
ATOM   2184 C  CG  . ARG A 1 343 ? 18.961  -9.271  8.260   1.00 11.40 ? 343 ARG A CG  1 
ATOM   2185 C  CD  . ARG A 1 343 ? 20.382  -9.748  8.572   1.00 10.84 ? 343 ARG A CD  1 
ATOM   2186 N  NE  . ARG A 1 343 ? 20.316  -10.891 9.514   1.00 12.06 ? 343 ARG A NE  1 
ATOM   2187 C  CZ  . ARG A 1 343 ? 20.292  -10.819 10.861  1.00 14.47 ? 343 ARG A CZ  1 
ATOM   2188 N  NH1 . ARG A 1 343 ? 20.069  -9.660  11.479  1.00 12.86 ? 343 ARG A NH1 1 
ATOM   2189 N  NH2 . ARG A 1 343 ? 20.448  -11.949 11.569  1.00 13.88 ? 343 ARG A NH2 1 
ATOM   2190 N  N   . GLY A 1 344 ? 15.922  -5.898  7.446   1.00 11.29 ? 344 GLY A N   1 
ATOM   2191 C  CA  . GLY A 1 344 ? 15.384  -4.714  8.095   1.00 14.26 ? 344 GLY A CA  1 
ATOM   2192 C  C   . GLY A 1 344 ? 14.496  -4.996  9.297   1.00 12.07 ? 344 GLY A C   1 
ATOM   2193 O  O   . GLY A 1 344 ? 14.085  -6.138  9.567   1.00 12.12 ? 344 GLY A O   1 
ATOM   2194 N  N   . TYR A 1 345 ? 14.210  -3.900  9.983   1.00 10.88 ? 345 TYR A N   1 
ATOM   2195 C  CA  . TYR A 1 345 ? 13.423  -3.861  11.212  1.00 10.39 ? 345 TYR A CA  1 
ATOM   2196 C  C   . TYR A 1 345 ? 12.477  -2.660  11.131  1.00 11.22 ? 345 TYR A C   1 
ATOM   2197 O  O   . TYR A 1 345 ? 12.813  -1.627  10.566  1.00 12.47 ? 345 TYR A O   1 
ATOM   2198 C  CB  . TYR A 1 345 ? 14.283  -3.717  12.460  1.00 11.91 ? 345 TYR A CB  1 
ATOM   2199 C  CG  . TYR A 1 345 ? 15.086  -4.941  12.748  1.00 11.43 ? 345 TYR A CG  1 
ATOM   2200 C  CD1 . TYR A 1 345 ? 16.231  -5.289  12.037  1.00 13.41 ? 345 TYR A CD1 1 
ATOM   2201 C  CD2 . TYR A 1 345 ? 14.686  -5.751  13.773  1.00 12.17 ? 345 TYR A CD2 1 
ATOM   2202 C  CE1 . TYR A 1 345 ? 16.921  -6.474  12.337  1.00 12.50 ? 345 TYR A CE1 1 
ATOM   2203 C  CE2 . TYR A 1 345 ? 15.397  -6.878  14.144  1.00 10.81 ? 345 TYR A CE2 1 
ATOM   2204 C  CZ  . TYR A 1 345 ? 16.531  -7.235  13.412  1.00 13.66 ? 345 TYR A CZ  1 
ATOM   2205 O  OH  . TYR A 1 345 ? 17.100  -8.463  13.715  1.00 13.75 ? 345 TYR A OH  1 
ATOM   2206 N  N   . SER A 1 346 ? 11.362  -2.729  11.846  1.00 12.56 ? 346 SER A N   1 
ATOM   2207 C  CA  . SER A 1 346 ? 10.456  -1.581  12.041  1.00 11.76 ? 346 SER A CA  1 
ATOM   2208 C  C   . SER A 1 346 ? 10.917  -0.690  13.180  1.00 13.61 ? 346 SER A C   1 
ATOM   2209 O  O   . SER A 1 346 ? 11.496  -1.150  14.171  1.00 14.30 ? 346 SER A O   1 
ATOM   2210 C  CB  . SER A 1 346 ? 9.058   -2.065  12.388  1.00 12.92 ? 346 SER A CB  1 
ATOM   2211 O  OG  . SER A 1 346 ? 8.506   -2.864  11.367  1.00 14.87 ? 346 SER A OG  1 
ATOM   2212 N  N   . PHE A 1 347 ? 10.482  0.577   13.101  1.00 12.06 ? 347 PHE A N   1 
ATOM   2213 C  CA  . PHE A 1 347 ? 10.715  1.480   14.209  1.00 12.88 ? 347 PHE A CA  1 
ATOM   2214 C  C   . PHE A 1 347 ? 9.495   2.387   14.397  1.00 12.83 ? 347 PHE A C   1 
ATOM   2215 O  O   . PHE A 1 347 ? 8.714   2.595   13.487  1.00 11.66 ? 347 PHE A O   1 
ATOM   2216 C  CB  . PHE A 1 347 ? 12.026  2.292   14.045  1.00 13.59 ? 347 PHE A CB  1 
ATOM   2217 C  CG  . PHE A 1 347 ? 12.006  3.307   12.949  1.00 14.94 ? 347 PHE A CG  1 
ATOM   2218 C  CD1 . PHE A 1 347 ? 11.493  4.596   13.187  1.00 16.41 ? 347 PHE A CD1 1 
ATOM   2219 C  CD2 . PHE A 1 347 ? 12.534  3.049   11.695  1.00 15.38 ? 347 PHE A CD2 1 
ATOM   2220 C  CE1 . PHE A 1 347 ? 11.337  5.496   12.136  1.00 19.87 ? 347 PHE A CE1 1 
ATOM   2221 C  CE2 . PHE A 1 347 ? 12.533  4.015   10.709  1.00 16.00 ? 347 PHE A CE2 1 
ATOM   2222 C  CZ  . PHE A 1 347 ? 11.856  5.198   10.902  1.00 19.79 ? 347 PHE A CZ  1 
ATOM   2223 N  N   . THR A 1 348 ? 9.381   2.940   15.608  1.00 16.03 ? 348 THR A N   1 
ATOM   2224 C  CA  . THR A 1 348 ? 8.520   4.077   15.891  1.00 15.00 ? 348 THR A CA  1 
ATOM   2225 C  C   . THR A 1 348 ? 9.286   4.913   16.914  1.00 21.04 ? 348 THR A C   1 
ATOM   2226 O  O   . THR A 1 348 ? 9.647   4.377   17.974  1.00 21.82 ? 348 THR A O   1 
ATOM   2227 C  CB  . THR A 1 348 ? 7.107   3.675   16.331  1.00 21.40 ? 348 THR A CB  1 
ATOM   2228 O  OG1 . THR A 1 348 ? 6.395   4.867   16.704  1.00 23.89 ? 348 THR A OG1 1 
ATOM   2229 C  CG2 . THR A 1 348 ? 7.025   2.747   17.523  1.00 22.70 ? 348 THR A CG2 1 
ATOM   2230 N  N   . ASP A 1 349 ? 9.411   6.192   16.612  1.00 18.99 ? 349 ASP A N   1 
ATOM   2231 C  CA  . ASP A 1 349 ? 10.167  7.135   17.440  1.00 29.44 ? 349 ASP A CA  1 
ATOM   2232 C  C   . ASP A 1 349 ? 9.192   8.207   17.938  1.00 29.81 ? 349 ASP A C   1 
ATOM   2233 O  O   . ASP A 1 349 ? 9.296   9.380   17.589  1.00 46.82 ? 349 ASP A O   1 
ATOM   2234 C  CB  . ASP A 1 349 ? 11.376  7.709   16.661  1.00 30.89 ? 349 ASP A CB  1 
ATOM   2235 C  CG  . ASP A 1 349 ? 12.470  6.660   16.356  1.00 34.22 ? 349 ASP A CG  1 
ATOM   2236 O  OD1 . ASP A 1 349 ? 12.477  5.546   16.942  1.00 38.55 ? 349 ASP A OD1 1 
ATOM   2237 O  OD2 . ASP A 1 349 ? 13.251  6.884   15.445  1.00 54.85 ? 349 ASP A OD2 1 
ATOM   2238 N  N   . GLY A 1 350 ? 8.131   7.779   18.590  1.00 22.79 ? 350 GLY A N   1 
ATOM   2239 C  CA  . GLY A 1 350 ? 7.219   8.672   19.261  1.00 23.48 ? 350 GLY A CA  1 
ATOM   2240 C  C   . GLY A 1 350 ? 6.098   9.195   18.340  1.00 20.34 ? 350 GLY A C   1 
ATOM   2241 O  O   . GLY A 1 350 ? 5.475   8.452   17.606  1.00 22.89 ? 350 GLY A O   1 
ATOM   2242 N  N   . THR A 1 351 ? 5.831   10.498  18.416  1.00 22.33 ? 351 THR A N   1 
ATOM   2243 C  CA  . THR A 1 351 ? 4.798   11.108  17.618  1.00 20.24 ? 351 THR A CA  1 
ATOM   2244 C  C   . THR A 1 351 ? 5.500   12.075  16.697  1.00 21.83 ? 351 THR A C   1 
ATOM   2245 O  O   . THR A 1 351 ? 6.677   12.360  16.849  1.00 21.90 ? 351 THR A O   1 
ATOM   2246 C  CB  . THR A 1 351 ? 3.743   11.851  18.440  1.00 21.90 ? 351 THR A CB  1 
ATOM   2247 O  OG1 . THR A 1 351 ? 4.406   12.818  19.246  1.00 27.26 ? 351 THR A OG1 1 
ATOM   2248 C  CG2 . THR A 1 351 ? 2.964   10.906  19.318  1.00 23.01 ? 351 THR A CG2 1 
ATOM   2249 N  N   . ASP A 1 352 ? 4.767   12.509  15.688  1.00 19.26 ? 352 ASP A N   1 
ATOM   2250 C  CA  . ASP A 1 352 ? 5.333   13.426  14.725  1.00 23.23 ? 352 ASP A CA  1 
ATOM   2251 C  C   . ASP A 1 352 ? 5.080   14.882  15.094  1.00 22.19 ? 352 ASP A C   1 
ATOM   2252 O  O   . ASP A 1 352 ? 5.397   15.766  14.287  1.00 24.50 ? 352 ASP A O   1 
ATOM   2253 C  CB  . ASP A 1 352 ? 4.769   13.165  13.322  1.00 23.00 ? 352 ASP A CB  1 
ATOM   2254 C  CG  . ASP A 1 352 ? 3.278   13.208  13.202  1.00 22.43 ? 352 ASP A CG  1 
ATOM   2255 O  OD1 . ASP A 1 352 ? 2.584   13.605  14.189  1.00 18.09 ? 352 ASP A OD1 1 
ATOM   2256 O  OD2 . ASP A 1 352 ? 2.830   12.816  12.111  1.00 24.34 ? 352 ASP A OD2 1 
ATOM   2257 N  N   . GLY A 1 353 ? 4.518   15.157  16.269  1.00 18.95 ? 353 GLY A N   1 
ATOM   2258 C  CA  . GLY A 1 353 ? 4.067   16.489  16.659  1.00 21.45 ? 353 GLY A CA  1 
ATOM   2259 C  C   . GLY A 1 353 ? 2.843   17.066  15.936  1.00 20.57 ? 353 GLY A C   1 
ATOM   2260 O  O   . GLY A 1 353 ? 2.408   18.198  16.227  1.00 19.16 ? 353 GLY A O   1 
ATOM   2261 N  N   . LEU A 1 354 ? 2.234   16.278  15.061  1.00 17.30 ? 354 LEU A N   1 
ATOM   2262 C  CA  . LEU A 1 354 ? 0.991   16.603  14.339  1.00 18.37 ? 354 LEU A CA  1 
ATOM   2263 C  C   . LEU A 1 354 ? -0.140  15.627  14.690  1.00 16.22 ? 354 LEU A C   1 
ATOM   2264 O  O   . LEU A 1 354 ? -1.083  15.421  13.949  1.00 16.77 ? 354 LEU A O   1 
ATOM   2265 C  CB  . LEU A 1 354 ? 1.332   16.535  12.847  1.00 19.09 ? 354 LEU A CB  1 
ATOM   2266 C  CG  . LEU A 1 354 ? 2.471   17.505  12.461  1.00 23.18 ? 354 LEU A CG  1 
ATOM   2267 C  CD1 . LEU A 1 354 ? 3.168   17.008  11.216  1.00 27.34 ? 354 LEU A CD1 1 
ATOM   2268 C  CD2 . LEU A 1 354 ? 1.918   18.912  12.303  1.00 27.54 ? 354 LEU A CD2 1 
ATOM   2269 N  N   . GLY A 1 355 ? -0.033  14.988  15.861  1.00 15.84 ? 355 GLY A N   1 
ATOM   2270 C  CA  . GLY A 1 355 ? -1.128  14.210  16.383  1.00 13.03 ? 355 GLY A CA  1 
ATOM   2271 C  C   . GLY A 1 355 ? -1.121  12.770  15.966  1.00 12.73 ? 355 GLY A C   1 
ATOM   2272 O  O   . GLY A 1 355 ? -2.119  12.080  16.169  1.00 14.04 ? 355 GLY A O   1 
ATOM   2273 N  N   . ARG A 1 356 ? -0.018  12.323  15.381  1.00 13.85 ? 356 ARG A N   1 
ATOM   2274 C  CA  . ARG A 1 356 ? 0.076   10.992  14.827  1.00 14.64 ? 356 ARG A CA  1 
ATOM   2275 C  C   . ARG A 1 356 ? 1.288   10.235  15.361  1.00 14.65 ? 356 ARG A C   1 
ATOM   2276 O  O   . ARG A 1 356 ? 2.318   10.805  15.683  1.00 17.26 ? 356 ARG A O   1 
ATOM   2277 C  CB  . ARG A 1 356 ? 0.209   11.051  13.305  1.00 16.34 ? 356 ARG A CB  1 
ATOM   2278 C  CG  . ARG A 1 356 ? -0.912  11.840  12.659  1.00 17.94 ? 356 ARG A CG  1 
ATOM   2279 C  CD  . ARG A 1 356 ? -0.707  11.859  11.181  1.00 17.25 ? 356 ARG A CD  1 
ATOM   2280 N  NE  . ARG A 1 356 ? 0.469   12.621  10.852  1.00 18.09 ? 356 ARG A NE  1 
ATOM   2281 C  CZ  . ARG A 1 356 ? 0.931   12.779  9.611   1.00 18.78 ? 356 ARG A CZ  1 
ATOM   2282 N  NH1 . ARG A 1 356 ? 0.162   12.486  8.570   1.00 15.76 ? 356 ARG A NH1 1 
ATOM   2283 N  NH2 . ARG A 1 356 ? 2.145   13.283  9.450   1.00 22.34 ? 356 ARG A NH2 1 
ATOM   2284 N  N   . LEU A 1 357 ? 1.170   8.909   15.337  1.00 15.09 ? 357 LEU A N   1 
ATOM   2285 C  CA  . LEU A 1 357 ? 2.369   8.116   15.583  1.00 17.63 ? 357 LEU A CA  1 
ATOM   2286 C  C   . LEU A 1 357 ? 3.343   8.264   14.426  1.00 19.34 ? 357 LEU A C   1 
ATOM   2287 O  O   . LEU A 1 357 ? 2.964   8.255   13.291  1.00 20.48 ? 357 LEU A O   1 
ATOM   2288 C  CB  . LEU A 1 357 ? 1.998   6.629   15.642  1.00 19.75 ? 357 LEU A CB  1 
ATOM   2289 C  CG  . LEU A 1 357 ? 1.020   6.173   16.691  1.00 24.13 ? 357 LEU A CG  1 
ATOM   2290 C  CD1 . LEU A 1 357 ? 0.826   4.672   16.467  1.00 28.16 ? 357 LEU A CD1 1 
ATOM   2291 C  CD2 . LEU A 1 357 ? 1.578   6.359   18.094  1.00 24.77 ? 357 LEU A CD2 1 
ATOM   2292 N  N   . ASP A 1 358 ? 4.594   8.263   14.750  1.00 16.05 ? 358 ASP A N   1 
ATOM   2293 C  CA  . ASP A 1 358 ? 5.680   8.192   13.816  1.00 21.32 ? 358 ASP A CA  1 
ATOM   2294 C  C   . ASP A 1 358 ? 5.951   6.722   13.555  1.00 26.79 ? 358 ASP A C   1 
ATOM   2295 O  O   . ASP A 1 358 ? 5.978   5.927   14.502  1.00 28.84 ? 358 ASP A O   1 
ATOM   2296 C  CB  . ASP A 1 358 ? 6.899   8.886   14.418  1.00 31.16 ? 358 ASP A CB  1 
ATOM   2297 C  CG  . ASP A 1 358 ? 8.169   8.534   13.676  1.00 39.10 ? 358 ASP A CG  1 
ATOM   2298 O  OD1 . ASP A 1 358 ? 8.786   7.429   13.963  1.00 39.86 ? 358 ASP A OD1 1 
ATOM   2299 O  OD2 . ASP A 1 358 ? 8.437   9.302   12.790  1.00 28.84 ? 358 ASP A OD2 1 
ATOM   2300 N  N   . ALA A 1 359 ? 6.110   6.353   12.296  1.00 18.94 ? 359 ALA A N   1 
ATOM   2301 C  CA  . ALA A 1 359 ? 6.356   4.945   12.012  1.00 20.62 ? 359 ALA A CA  1 
ATOM   2302 C  C   . ALA A 1 359 ? 7.286   4.841   10.827  1.00 16.30 ? 359 ALA A C   1 
ATOM   2303 O  O   . ALA A 1 359 ? 7.267   5.672   9.938   1.00 15.76 ? 359 ALA A O   1 
ATOM   2304 C  CB  . ALA A 1 359 ? 5.089   4.192   11.729  1.00 23.66 ? 359 ALA A CB  1 
ATOM   2305 N  N   . GLY A 1 360 ? 8.087   3.771   10.833  1.00 15.06 ? 360 GLY A N   1 
ATOM   2306 C  CA  . GLY A 1 360 ? 9.001   3.567   9.750   1.00 15.34 ? 360 GLY A CA  1 
ATOM   2307 C  C   . GLY A 1 360 ? 9.540   2.147   9.698   1.00 14.75 ? 360 GLY A C   1 
ATOM   2308 O  O   . GLY A 1 360 ? 9.147   1.265   10.476  1.00 15.46 ? 360 GLY A O   1 
ATOM   2309 N  N   . LEU A 1 361 ? 10.414  2.012   8.707   1.00 12.44 ? 361 LEU A N   1 
ATOM   2310 C  CA  . LEU A 1 361 ? 11.161  0.793   8.432   1.00 12.01 ? 361 LEU A CA  1 
ATOM   2311 C  C   . LEU A 1 361 ? 12.614  1.211   8.283   1.00 10.82 ? 361 LEU A C   1 
ATOM   2312 O  O   . LEU A 1 361 ? 12.964  2.069   7.504   1.00 12.09 ? 361 LEU A O   1 
ATOM   2313 C  CB  . LEU A 1 361 ? 10.593  0.074   7.187   1.00 13.16 ? 361 LEU A CB  1 
ATOM   2314 C  CG  . LEU A 1 361 ? 10.911  -1.384  7.017   1.00 14.99 ? 361 LEU A CG  1 
ATOM   2315 C  CD1 . LEU A 1 361 ? 9.828   -2.138  6.247   1.00 17.25 ? 361 LEU A CD1 1 
ATOM   2316 C  CD2 . LEU A 1 361 ? 12.210  -1.518  6.312   1.00 17.21 ? 361 LEU A CD2 1 
ATOM   2317 N  N   . PHE A 1 362 ? 13.458  0.564   9.076   1.00 11.65 ? 362 PHE A N   1 
ATOM   2318 C  CA  . PHE A 1 362 ? 14.893  0.697   8.952   1.00 12.17 ? 362 PHE A CA  1 
ATOM   2319 C  C   . PHE A 1 362 ? 15.357  -0.442  8.049   1.00 13.25 ? 362 PHE A C   1 
ATOM   2320 O  O   . PHE A 1 362 ? 15.511  -1.625  8.421   1.00 13.40 ? 362 PHE A O   1 
ATOM   2321 C  CB  . PHE A 1 362 ? 15.526  0.701   10.354  1.00 13.27 ? 362 PHE A CB  1 
ATOM   2322 C  CG  . PHE A 1 362 ? 16.995  1.012   10.303  1.00 16.06 ? 362 PHE A CG  1 
ATOM   2323 C  CD1 . PHE A 1 362 ? 17.444  2.282   9.918   1.00 16.82 ? 362 PHE A CD1 1 
ATOM   2324 C  CD2 . PHE A 1 362 ? 17.933  0.071   10.711  1.00 17.45 ? 362 PHE A CD2 1 
ATOM   2325 C  CE1 . PHE A 1 362 ? 18.798  2.579   9.904   1.00 18.09 ? 362 PHE A CE1 1 
ATOM   2326 C  CE2 . PHE A 1 362 ? 19.287  0.388   10.701  1.00 17.38 ? 362 PHE A CE2 1 
ATOM   2327 C  CZ  . PHE A 1 362 ? 19.711  1.617   10.285  1.00 15.56 ? 362 PHE A CZ  1 
ATOM   2328 N  N   . PHE A 1 363 ? 15.539  -0.085  6.798   1.00 12.91 ? 363 PHE A N   1 
ATOM   2329 C  CA  . PHE A 1 363 ? 15.853  -1.026  5.743   1.00 11.94 ? 363 PHE A CA  1 
ATOM   2330 C  C   . PHE A 1 363 ? 17.353  -1.311  5.735   1.00 11.97 ? 363 PHE A C   1 
ATOM   2331 O  O   . PHE A 1 363 ? 18.179  -0.402  5.726   1.00 13.40 ? 363 PHE A O   1 
ATOM   2332 C  CB  . PHE A 1 363 ? 15.378  -0.381  4.427   1.00 12.04 ? 363 PHE A CB  1 
ATOM   2333 C  CG  . PHE A 1 363 ? 15.587  -1.308  3.254   1.00 13.37 ? 363 PHE A CG  1 
ATOM   2334 C  CD1 . PHE A 1 363 ? 14.634  -2.272  2.957   1.00 14.39 ? 363 PHE A CD1 1 
ATOM   2335 C  CD2 . PHE A 1 363 ? 16.741  -1.228  2.478   1.00 14.32 ? 363 PHE A CD2 1 
ATOM   2336 C  CE1 . PHE A 1 363 ? 14.815  -3.126  1.856   1.00 14.96 ? 363 PHE A CE1 1 
ATOM   2337 C  CE2 . PHE A 1 363 ? 16.934  -2.115  1.420   1.00 14.78 ? 363 PHE A CE2 1 
ATOM   2338 C  CZ  . PHE A 1 363 ? 15.948  -3.010  1.080   1.00 14.17 ? 363 PHE A CZ  1 
ATOM   2339 N  N   . LEU A 1 364 ? 17.704  -2.597  5.760   1.00 10.71 ? 364 LEU A N   1 
ATOM   2340 C  CA  . LEU A 1 364 ? 19.088  -3.035  5.750   1.00 13.23 ? 364 LEU A CA  1 
ATOM   2341 C  C   . LEU A 1 364 ? 19.226  -4.045  4.657   1.00 12.60 ? 364 LEU A C   1 
ATOM   2342 O  O   . LEU A 1 364 ? 18.446  -4.980  4.630   1.00 14.27 ? 364 LEU A O   1 
ATOM   2343 C  CB  . LEU A 1 364 ? 19.498  -3.685  7.082   1.00 12.61 ? 364 LEU A CB  1 
ATOM   2344 C  CG  . LEU A 1 364 ? 19.489  -2.775  8.305   1.00 12.72 ? 364 LEU A CG  1 
ATOM   2345 C  CD1 . LEU A 1 364 ? 19.743  -3.544  9.589   1.00 12.82 ? 364 LEU A CD1 1 
ATOM   2346 C  CD2 . LEU A 1 364 ? 20.546  -1.733  8.148   1.00 17.80 ? 364 LEU A CD2 1 
ATOM   2347 N  N   . ALA A 1 365 ? 20.161  -3.808  3.737   1.00 14.56 ? 365 ALA A N   1 
ATOM   2348 C  CA  . ALA A 1 365 ? 20.384  -4.772  2.663   1.00 15.53 ? 365 ALA A CA  1 
ATOM   2349 C  C   . ALA A 1 365 ? 21.882  -5.091  2.613   1.00 14.33 ? 365 ALA A C   1 
ATOM   2350 O  O   . ALA A 1 365 ? 22.730  -4.192  2.569   1.00 15.65 ? 365 ALA A O   1 
ATOM   2351 C  CB  . ALA A 1 365 ? 19.894  -4.275  1.340   1.00 17.09 ? 365 ALA A CB  1 
ATOM   2352 N  N   . TYR A 1 366 ? 22.147  -6.397  2.508   1.00 13.99 ? 366 TYR A N   1 
ATOM   2353 C  CA  . TYR A 1 366 ? 23.486  -6.914  2.300   1.00 13.91 ? 366 TYR A CA  1 
ATOM   2354 C  C   . TYR A 1 366 ? 23.598  -7.448  0.877   1.00 14.49 ? 366 TYR A C   1 
ATOM   2355 O  O   . TYR A 1 366 ? 22.664  -8.038  0.330   1.00 14.33 ? 366 TYR A O   1 
ATOM   2356 C  CB  . TYR A 1 366 ? 23.813  -7.999  3.312   1.00 14.35 ? 366 TYR A CB  1 
ATOM   2357 C  CG  . TYR A 1 366 ? 23.970  -7.536  4.741   1.00 13.38 ? 366 TYR A CG  1 
ATOM   2358 C  CD1 . TYR A 1 366 ? 22.867  -7.457  5.604   1.00 15.34 ? 366 TYR A CD1 1 
ATOM   2359 C  CD2 . TYR A 1 366 ? 25.208  -7.167  5.223   1.00 15.69 ? 366 TYR A CD2 1 
ATOM   2360 C  CE1 . TYR A 1 366 ? 23.017  -7.015  6.912   1.00 16.17 ? 366 TYR A CE1 1 
ATOM   2361 C  CE2 . TYR A 1 366 ? 25.372  -6.741  6.535   1.00 15.49 ? 366 TYR A CE2 1 
ATOM   2362 C  CZ  . TYR A 1 366 ? 24.281  -6.668  7.379   1.00 18.04 ? 366 TYR A CZ  1 
ATOM   2363 O  OH  . TYR A 1 366 ? 24.446  -6.168  8.651   1.00 18.12 ? 366 TYR A OH  1 
ATOM   2364 N  N   . GLN A 1 367 ? 24.790  -7.234  0.311   1.00 15.56 ? 367 GLN A N   1 
ATOM   2365 C  CA  . GLN A 1 367 ? 25.043  -7.612  -1.072  1.00 17.12 ? 367 GLN A CA  1 
ATOM   2366 C  C   . GLN A 1 367 ? 26.541  -7.668  -1.313  1.00 13.61 ? 367 GLN A C   1 
ATOM   2367 O  O   . GLN A 1 367 ? 27.335  -6.996  -0.654  1.00 14.21 ? 367 GLN A O   1 
ATOM   2368 C  CB  . GLN A 1 367 ? 24.383  -6.623  -2.062  1.00 14.80 ? 367 GLN A CB  1 
ATOM   2369 C  CG  . GLN A 1 367 ? 24.864  -5.195  -1.939  1.00 17.19 ? 367 GLN A CG  1 
ATOM   2370 C  CD  . GLN A 1 367 ? 23.878  -4.252  -1.322  1.00 21.95 ? 367 GLN A CD  1 
ATOM   2371 O  OE1 . GLN A 1 367 ? 23.006  -3.775  -2.024  1.00 24.91 ? 367 GLN A OE1 1 
ATOM   2372 N  NE2 . GLN A 1 367 ? 23.960  -3.969  -0.021  1.00 17.08 ? 367 GLN A NE2 1 
ATOM   2373 N  N   . ARG A 1 368 ? 26.871  -8.355  -2.384  1.00 15.85 ? 368 ARG A N   1 
ATOM   2374 C  CA  . ARG A 1 368 ? 28.264  -8.554  -2.799  1.00 16.41 ? 368 ARG A CA  1 
ATOM   2375 C  C   . ARG A 1 368 ? 28.921  -7.299  -3.373  1.00 18.25 ? 368 ARG A C   1 
ATOM   2376 O  O   . ARG A 1 368 ? 30.125  -7.181  -3.359  1.00 16.31 ? 368 ARG A O   1 
ATOM   2377 C  CB  . ARG A 1 368 ? 28.262  -9.717  -3.803  1.00 17.62 ? 368 ARG A CB  1 
ATOM   2378 C  CG  . ARG A 1 368 ? 29.599  -10.020 -4.445  1.00 16.79 ? 368 ARG A CG  1 
ATOM   2379 C  CD  . ARG A 1 368 ? 29.480  -11.349 -5.132  1.00 17.90 ? 368 ARG A CD  1 
ATOM   2380 N  NE  . ARG A 1 368 ? 30.726  -11.679 -5.867  1.00 20.58 ? 368 ARG A NE  1 
ATOM   2381 C  CZ  . ARG A 1 368 ? 30.852  -12.760 -6.637  1.00 28.52 ? 368 ARG A CZ  1 
ATOM   2382 N  NH1 . ARG A 1 368 ? 29.794  -13.497 -6.921  1.00 30.55 ? 368 ARG A NH1 1 
ATOM   2383 N  NH2 . ARG A 1 368 ? 32.031  -13.095 -7.131  1.00 27.65 ? 368 ARG A NH2 1 
ATOM   2384 N  N   . ASP A 1 369 ? 28.114  -6.422  -3.940  1.00 17.39 ? 369 ASP A N   1 
ATOM   2385 C  CA  . ASP A 1 369 ? 28.536  -5.182  -4.537  1.00 19.38 ? 369 ASP A CA  1 
ATOM   2386 C  C   . ASP A 1 369 ? 27.351  -4.245  -4.539  1.00 17.76 ? 369 ASP A C   1 
ATOM   2387 O  O   . ASP A 1 369 ? 26.302  -4.572  -5.085  1.00 17.62 ? 369 ASP A O   1 
ATOM   2388 C  CB  . ASP A 1 369 ? 29.036  -5.447  -5.954  1.00 18.25 ? 369 ASP A CB  1 
ATOM   2389 C  CG  . ASP A 1 369 ? 29.766  -4.283  -6.610  1.00 20.99 ? 369 ASP A CG  1 
ATOM   2390 O  OD1 . ASP A 1 369 ? 29.397  -3.125  -6.397  1.00 18.91 ? 369 ASP A OD1 1 
ATOM   2391 O  OD2 . ASP A 1 369 ? 30.728  -4.591  -7.310  1.00 24.80 ? 369 ASP A OD2 1 
ATOM   2392 N  N   . ILE A 1 370 ? 27.514  -3.073  -3.940  1.00 16.49 ? 370 ILE A N   1 
ATOM   2393 C  CA  . ILE A 1 370 ? 26.405  -2.103  -3.903  1.00 17.69 ? 370 ILE A CA  1 
ATOM   2394 C  C   . ILE A 1 370 ? 25.942  -1.700  -5.311  1.00 20.12 ? 370 ILE A C   1 
ATOM   2395 O  O   . ILE A 1 370 ? 24.753  -1.426  -5.546  1.00 18.56 ? 370 ILE A O   1 
ATOM   2396 C  CB  . ILE A 1 370 ? 26.859  -0.905  -3.066  1.00 18.52 ? 370 ILE A CB  1 
ATOM   2397 C  CG1 . ILE A 1 370 ? 26.943  -1.320  -1.582  1.00 20.14 ? 370 ILE A CG1 1 
ATOM   2398 C  CG2 . ILE A 1 370 ? 25.919  0.277   -3.234  1.00 20.84 ? 370 ILE A CG2 1 
ATOM   2399 C  CD1 . ILE A 1 370 ? 27.410  -0.265  -0.651  1.00 19.61 ? 370 ILE A CD1 1 
ATOM   2400 N  N   . ARG A 1 371 ? 26.891  -1.671  -6.248  1.00 15.81 ? 371 ARG A N   1 
ATOM   2401 C  CA  . ARG A 1 371 ? 26.591  -1.202  -7.592  1.00 22.59 ? 371 ARG A CA  1 
ATOM   2402 C  C   . ARG A 1 371 ? 25.714  -2.183  -8.357  1.00 23.54 ? 371 ARG A C   1 
ATOM   2403 O  O   . ARG A 1 371 ? 25.037  -1.781  -9.303  1.00 22.19 ? 371 ARG A O   1 
ATOM   2404 C  CB  . ARG A 1 371 ? 27.921  -0.994  -8.338  1.00 22.96 ? 371 ARG A CB  1 
ATOM   2405 C  CG  . ARG A 1 371 ? 28.814  0.081   -7.726  1.00 24.67 ? 371 ARG A CG  1 
ATOM   2406 C  CD  . ARG A 1 371 ? 30.170  0.074   -8.420  1.00 26.02 ? 371 ARG A CD  1 
ATOM   2407 N  NE  . ARG A 1 371 ? 30.858  -1.204  -8.167  1.00 28.15 ? 371 ARG A NE  1 
ATOM   2408 C  CZ  . ARG A 1 371 ? 32.019  -1.570  -8.682  1.00 33.69 ? 371 ARG A CZ  1 
ATOM   2409 N  NH1 . ARG A 1 371 ? 32.600  -0.810  -9.593  1.00 31.43 ? 371 ARG A NH1 1 
ATOM   2410 N  NH2 . ARG A 1 371 ? 32.562  -2.729  -8.332  1.00 26.68 ? 371 ARG A NH2 1 
ATOM   2411 N  N   . THR A 1 372 ? 25.738  -3.459  -7.977  1.00 18.85 ? 372 THR A N   1 
ATOM   2412 C  CA  . THR A 1 372 ? 24.986  -4.506  -8.648  1.00 21.81 ? 372 THR A CA  1 
ATOM   2413 C  C   . THR A 1 372 ? 23.843  -5.050  -7.773  1.00 21.53 ? 372 THR A C   1 
ATOM   2414 O  O   . THR A 1 372 ? 23.148  -6.003  -8.152  1.00 22.67 ? 372 THR A O   1 
ATOM   2415 C  CB  . THR A 1 372 ? 25.873  -5.685  -9.093  1.00 23.00 ? 372 THR A CB  1 
ATOM   2416 O  OG1 . THR A 1 372 ? 26.456  -6.296  -7.945  1.00 21.05 ? 372 THR A OG1 1 
ATOM   2417 C  CG2 . THR A 1 372 ? 26.938  -5.237  -10.067 1.00 24.09 ? 372 THR A CG2 1 
ATOM   2418 N  N   . GLY A 1 373 ? 23.663  -4.478  -6.586  1.00 18.46 ? 373 GLY A N   1 
ATOM   2419 C  CA  . GLY A 1 373 ? 22.638  -4.980  -5.699  1.00 19.85 ? 373 GLY A CA  1 
ATOM   2420 C  C   . GLY A 1 373 ? 21.619  -3.865  -5.502  1.00 19.52 ? 373 GLY A C   1 
ATOM   2421 O  O   . GLY A 1 373 ? 20.686  -3.708  -6.298  1.00 17.08 ? 373 GLY A O   1 
ATOM   2422 N  N   . PHE A 1 374 ? 21.814  -3.106  -4.428  1.00 16.60 ? 374 PHE A N   1 
ATOM   2423 C  CA  . PHE A 1 374 ? 20.847  -2.065  -4.038  1.00 15.91 ? 374 PHE A CA  1 
ATOM   2424 C  C   . PHE A 1 374 ? 20.645  -1.011  -5.142  1.00 16.89 ? 374 PHE A C   1 
ATOM   2425 O  O   . PHE A 1 374 ? 19.542  -0.604  -5.417  1.00 16.56 ? 374 PHE A O   1 
ATOM   2426 C  CB  . PHE A 1 374 ? 21.275  -1.364  -2.758  1.00 16.07 ? 374 PHE A CB  1 
ATOM   2427 C  CG  . PHE A 1 374 ? 20.354  -0.255  -2.302  1.00 13.87 ? 374 PHE A CG  1 
ATOM   2428 C  CD1 . PHE A 1 374 ? 19.177  -0.551  -1.629  1.00 16.51 ? 374 PHE A CD1 1 
ATOM   2429 C  CD2 . PHE A 1 374 ? 20.611  1.081   -2.646  1.00 13.18 ? 374 PHE A CD2 1 
ATOM   2430 C  CE1 . PHE A 1 374 ? 18.332  0.477   -1.229  1.00 16.84 ? 374 PHE A CE1 1 
ATOM   2431 C  CE2 . PHE A 1 374 ? 19.763  2.095   -2.235  1.00 14.72 ? 374 PHE A CE2 1 
ATOM   2432 C  CZ  . PHE A 1 374 ? 18.616  1.787   -1.538  1.00 18.81 ? 374 PHE A CZ  1 
ATOM   2433 N  N   . VAL A 1 375 ? 21.689  -0.507  -5.750  1.00 17.60 ? 375 VAL A N   1 
ATOM   2434 C  CA  . VAL A 1 375 ? 21.564  0.615   -6.695  1.00 17.42 ? 375 VAL A CA  1 
ATOM   2435 C  C   . VAL A 1 375 ? 20.630  0.283   -7.856  1.00 17.63 ? 375 VAL A C   1 
ATOM   2436 O  O   . VAL A 1 375 ? 19.698  1.041   -8.056  1.00 17.08 ? 375 VAL A O   1 
ATOM   2437 C  CB  . VAL A 1 375 ? 22.954  1.123   -7.139  1.00 18.79 ? 375 VAL A CB  1 
ATOM   2438 C  CG1 . VAL A 1 375 ? 22.849  2.079   -8.327  1.00 22.78 ? 375 VAL A CG1 1 
ATOM   2439 C  CG2 . VAL A 1 375 ? 23.621  1.856   -5.963  1.00 21.34 ? 375 VAL A CG2 1 
ATOM   2440 N  N   . PRO A 1 376 ? 20.808  -0.811  -8.628  1.00 18.08 ? 376 PRO A N   1 
ATOM   2441 C  CA  . PRO A 1 376 ? 19.878  -1.097  -9.743  1.00 20.07 ? 376 PRO A CA  1 
ATOM   2442 C  C   . PRO A 1 376 ? 18.445  -1.347  -9.299  1.00 16.11 ? 376 PRO A C   1 
ATOM   2443 O  O   . PRO A 1 376 ? 17.537  -0.766  -9.880  1.00 16.22 ? 376 PRO A O   1 
ATOM   2444 C  CB  . PRO A 1 376 ? 20.419  -2.322  -10.490 1.00 20.79 ? 376 PRO A CB  1 
ATOM   2445 C  CG  . PRO A 1 376 ? 21.519  -2.834  -9.562  1.00 23.35 ? 376 PRO A CG  1 
ATOM   2446 C  CD  . PRO A 1 376 ? 21.996  -1.657  -8.739  1.00 19.49 ? 376 PRO A CD  1 
ATOM   2447 N  N   . VAL A 1 377 ? 18.272  -2.006  -8.126  1.00 14.79 ? 377 VAL A N   1 
ATOM   2448 C  CA  . VAL A 1 377 ? 16.940  -2.251  -7.638  1.00 17.62 ? 377 VAL A CA  1 
ATOM   2449 C  C   . VAL A 1 377 ? 16.284  -0.923  -7.271  1.00 15.78 ? 377 VAL A C   1 
ATOM   2450 O  O   . VAL A 1 377 ? 15.153  -0.646  -7.681  1.00 16.81 ? 377 VAL A O   1 
ATOM   2451 C  CB  . VAL A 1 377 ? 16.904  -3.336  -6.531  1.00 15.62 ? 377 VAL A CB  1 
ATOM   2452 C  CG1 . VAL A 1 377 ? 15.475  -3.514  -6.004  1.00 14.72 ? 377 VAL A CG1 1 
ATOM   2453 C  CG2 . VAL A 1 377 ? 17.470  -4.673  -7.014  1.00 17.13 ? 377 VAL A CG2 1 
ATOM   2454 N  N   . GLN A 1 378 ? 16.923  -0.107  -6.422  1.00 14.51 ? 378 GLN A N   1 
ATOM   2455 C  CA  . GLN A 1 378 ? 16.274  1.144   -6.026  1.00 15.37 ? 378 GLN A CA  1 
ATOM   2456 C  C   . GLN A 1 378 ? 16.048  2.077   -7.205  1.00 14.94 ? 378 GLN A C   1 
ATOM   2457 O  O   . GLN A 1 378 ? 15.077  2.810   -7.240  1.00 16.10 ? 378 GLN A O   1 
ATOM   2458 C  CB  . GLN A 1 378 ? 17.189  1.826   -4.989  1.00 16.94 ? 378 GLN A CB  1 
ATOM   2459 C  CG  . GLN A 1 378 ? 16.683  3.172   -4.505  1.00 16.37 ? 378 GLN A CG  1 
ATOM   2460 C  CD  . GLN A 1 378 ? 15.354  3.137   -3.769  1.00 21.82 ? 378 GLN A CD  1 
ATOM   2461 O  OE1 . GLN A 1 378 ? 15.025  2.184   -3.085  1.00 21.72 ? 378 GLN A OE1 1 
ATOM   2462 N  NE2 . GLN A 1 378 ? 14.529  4.164   -3.914  1.00 26.81 ? 378 GLN A NE2 1 
ATOM   2463 N  N   . ARG A 1 379 ? 16.993  2.123   -8.144  1.00 16.39 ? 379 ARG A N   1 
ATOM   2464 C  CA  . ARG A 1 379 ? 16.759  2.870   -9.394  1.00 17.79 ? 379 ARG A CA  1 
ATOM   2465 C  C   . ARG A 1 379 ? 15.471  2.414   -10.097 1.00 15.49 ? 379 ARG A C   1 
ATOM   2466 O  O   . ARG A 1 379 ? 14.675  3.255   -10.534 1.00 15.65 ? 379 ARG A O   1 
ATOM   2467 C  CB  . ARG A 1 379 ? 17.926  2.689   -10.381 1.00 22.76 ? 379 ARG A CB  1 
ATOM   2468 C  CG  . ARG A 1 379 ? 19.117  3.582   -10.139 1.00 30.14 ? 379 ARG A CG  1 
ATOM   2469 C  CD  . ARG A 1 379 ? 19.825  3.944   -11.443 1.00 38.98 ? 379 ARG A CD  1 
ATOM   2470 N  NE  . ARG A 1 379 ? 21.195  4.364   -11.160 1.00 43.54 ? 379 ARG A NE  1 
ATOM   2471 C  CZ  . ARG A 1 379 ? 21.618  5.632   -11.035 1.00 58.40 ? 379 ARG A CZ  1 
ATOM   2472 N  NH1 . ARG A 1 379 ? 20.850  6.577   -10.508 1.00 55.17 ? 379 ARG A NH1 1 
ATOM   2473 N  NH2 . ARG A 1 379 ? 22.838  5.956   -11.428 1.00 67.22 ? 379 ARG A NH2 1 
ATOM   2474 N  N   . ASN A 1 380 ? 15.181  1.098   -10.113 1.00 15.49 ? 380 ASN A N   1 
ATOM   2475 C  CA  . ASN A 1 380 ? 13.978  0.595   -10.746 1.00 14.73 ? 380 ASN A CA  1 
ATOM   2476 C  C   . ASN A 1 380 ? 12.724  0.945   -9.951  1.00 15.59 ? 380 ASN A C   1 
ATOM   2477 O  O   . ASN A 1 380 ? 11.602  0.823   -10.484 1.00 16.51 ? 380 ASN A O   1 
ATOM   2478 C  CB  . ASN A 1 380 ? 14.070  -0.914  -10.943 1.00 17.31 ? 380 ASN A CB  1 
ATOM   2479 C  CG  . ASN A 1 380 ? 13.378  -1.380  -12.187 1.00 20.88 ? 380 ASN A CG  1 
ATOM   2480 O  OD1 . ASN A 1 380 ? 13.510  -0.700  -13.222 1.00 18.65 ? 380 ASN A OD1 1 
ATOM   2481 N  ND2 . ASN A 1 380 ? 12.604  -2.455  -12.060 1.00 17.07 ? 380 ASN A ND2 1 
ATOM   2482 N  N   . LEU A 1 381 ? 12.906  1.309   -8.664  1.00 14.00 ? 381 LEU A N   1 
ATOM   2483 C  CA  . LEU A 1 381 ? 11.759  1.674   -7.865  1.00 13.92 ? 381 LEU A CA  1 
ATOM   2484 C  C   . LEU A 1 381 ? 11.325  3.122   -8.066  1.00 15.47 ? 381 LEU A C   1 
ATOM   2485 O  O   . LEU A 1 381 ? 10.451  3.605   -7.340  1.00 16.44 ? 381 LEU A O   1 
ATOM   2486 C  CB  . LEU A 1 381 ? 11.986  1.357   -6.388  1.00 15.27 ? 381 LEU A CB  1 
ATOM   2487 C  CG  . LEU A 1 381 ? 12.273  -0.118  -6.046  1.00 19.11 ? 381 LEU A CG  1 
ATOM   2488 C  CD1 . LEU A 1 381 ? 12.428  -0.236  -4.506  1.00 18.49 ? 381 LEU A CD1 1 
ATOM   2489 C  CD2 . LEU A 1 381 ? 11.188  -1.054  -6.538  1.00 18.80 ? 381 LEU A CD2 1 
ATOM   2490 N  N   . ALA A 1 382 ? 11.944  3.845   -9.016  1.00 17.16 ? 382 ALA A N   1 
ATOM   2491 C  CA  . ALA A 1 382 ? 11.586  5.226   -9.290  1.00 18.52 ? 382 ALA A CA  1 
ATOM   2492 C  C   . ALA A 1 382 ? 10.070  5.383   -9.507  1.00 18.35 ? 382 ALA A C   1 
ATOM   2493 O  O   . ALA A 1 382 ? 9.512   6.411   -9.140  1.00 21.21 ? 382 ALA A O   1 
ATOM   2494 C  CB  . ALA A 1 382 ? 12.312  5.737   -10.510 1.00 19.83 ? 382 ALA A CB  1 
ATOM   2495 N  N   . THR A 1 383 ? 9.427   4.388   -10.096 1.00 16.25 ? 383 THR A N   1 
ATOM   2496 C  CA  . THR A 1 383 ? 8.005   4.468   -10.456 1.00 19.54 ? 383 THR A CA  1 
ATOM   2497 C  C   . THR A 1 383 ? 7.130   3.638   -9.540  1.00 17.60 ? 383 THR A C   1 
ATOM   2498 O  O   . THR A 1 383 ? 5.941   3.486   -9.781  1.00 17.52 ? 383 THR A O   1 
ATOM   2499 C  CB  . THR A 1 383 ? 7.789   4.007   -11.907 1.00 20.60 ? 383 THR A CB  1 
ATOM   2500 O  OG1 . THR A 1 383 ? 8.202   2.649   -12.082 1.00 18.79 ? 383 THR A OG1 1 
ATOM   2501 C  CG2 . THR A 1 383 ? 8.602   4.801   -12.895 1.00 25.09 ? 383 THR A CG2 1 
ATOM   2502 N  N   . ASP A 1 384 ? 7.717   3.098   -8.476  1.00 14.33 ? 384 ASP A N   1 
ATOM   2503 C  CA  . ASP A 1 384 ? 6.965   2.261   -7.554  1.00 15.51 ? 384 ASP A CA  1 
ATOM   2504 C  C   . ASP A 1 384 ? 5.748   2.990   -7.011  1.00 14.48 ? 384 ASP A C   1 
ATOM   2505 O  O   . ASP A 1 384 ? 5.867   4.107   -6.479  1.00 13.75 ? 384 ASP A O   1 
ATOM   2506 C  CB  . ASP A 1 384 ? 7.952   1.891   -6.428  1.00 15.24 ? 384 ASP A CB  1 
ATOM   2507 C  CG  . ASP A 1 384 ? 7.572   0.757   -5.508  1.00 14.90 ? 384 ASP A CG  1 
ATOM   2508 O  OD1 . ASP A 1 384 ? 6.373   0.292   -5.542  1.00 13.84 ? 384 ASP A OD1 1 
ATOM   2509 O  OD2 . ASP A 1 384 ? 8.464   0.429   -4.682  1.00 14.96 ? 384 ASP A OD2 1 
ATOM   2510 N  N   . ALA A 1 385 ? 4.625   2.278   -7.021  1.00 15.02 ? 385 ALA A N   1 
ATOM   2511 C  CA  . ALA A 1 385 ? 3.397   2.685   -6.377  1.00 15.47 ? 385 ALA A CA  1 
ATOM   2512 C  C   . ALA A 1 385 ? 3.596   2.949   -4.873  1.00 15.11 ? 385 ALA A C   1 
ATOM   2513 O  O   . ALA A 1 385 ? 2.866   3.729   -4.268  1.00 15.74 ? 385 ALA A O   1 
ATOM   2514 C  CB  . ALA A 1 385 ? 2.359   1.631   -6.611  1.00 16.53 ? 385 ALA A CB  1 
ATOM   2515 N  N   . LEU A 1 386 ? 4.590   2.281   -4.251  1.00 14.13 ? 386 LEU A N   1 
ATOM   2516 C  CA  . LEU A 1 386 ? 4.824   2.422   -2.812  1.00 14.57 ? 386 LEU A CA  1 
ATOM   2517 C  C   . LEU A 1 386 ? 5.368   3.820   -2.492  1.00 16.51 ? 386 LEU A C   1 
ATOM   2518 O  O   . LEU A 1 386 ? 5.244   4.282   -1.372  1.00 11.97 ? 386 LEU A O   1 
ATOM   2519 C  CB  . LEU A 1 386 ? 5.767   1.306   -2.375  1.00 13.97 ? 386 LEU A CB  1 
ATOM   2520 C  CG  . LEU A 1 386 ? 6.153   1.273   -0.890  1.00 15.88 ? 386 LEU A CG  1 
ATOM   2521 C  CD1 . LEU A 1 386 ? 4.943   1.020   -0.057  1.00 13.80 ? 386 LEU A CD1 1 
ATOM   2522 C  CD2 . LEU A 1 386 ? 7.191   0.162   -0.672  1.00 15.20 ? 386 LEU A CD2 1 
ATOM   2523 N  N   . ASN A 1 387 ? 5.927   4.522   -3.482  1.00 14.54 ? 387 ASN A N   1 
ATOM   2524 C  CA  . ASN A 1 387 ? 6.563   5.804   -3.251  1.00 16.56 ? 387 ASN A CA  1 
ATOM   2525 C  C   . ASN A 1 387 ? 5.562   6.812   -2.688  1.00 15.59 ? 387 ASN A C   1 
ATOM   2526 O  O   . ASN A 1 387 ? 5.964   7.734   -1.985  1.00 14.42 ? 387 ASN A O   1 
ATOM   2527 C  CB  . ASN A 1 387 ? 7.269   6.365   -4.476  1.00 17.19 ? 387 ASN A CB  1 
ATOM   2528 C  CG  . ASN A 1 387 ? 8.504   5.583   -4.858  1.00 17.90 ? 387 ASN A CG  1 
ATOM   2529 O  OD1 . ASN A 1 387 ? 9.089   4.923   -4.023  1.00 22.14 ? 387 ASN A OD1 1 
ATOM   2530 N  ND2 . ASN A 1 387 ? 8.920   5.662   -6.111  1.00 16.68 ? 387 ASN A ND2 1 
ATOM   2531 N  N   . GLU A 1 388 ? 4.250   6.648   -2.978  1.00 14.83 ? 388 GLU A N   1 
ATOM   2532 C  CA  . GLU A 1 388 ? 3.263   7.546   -2.433  1.00 17.74 ? 388 GLU A CA  1 
ATOM   2533 C  C   . GLU A 1 388 ? 3.185   7.474   -0.897  1.00 19.44 ? 388 GLU A C   1 
ATOM   2534 O  O   . GLU A 1 388 ? 2.601   8.365   -0.247  1.00 18.98 ? 388 GLU A O   1 
ATOM   2535 C  CB  . GLU A 1 388 ? 1.894   7.144   -3.003  1.00 23.84 ? 388 GLU A CB  1 
ATOM   2536 C  CG  . GLU A 1 388 ? 0.727   7.988   -2.504  1.00 37.20 ? 388 GLU A CG  1 
ATOM   2537 C  CD  . GLU A 1 388 ? 0.767   9.452   -2.961  1.00 44.79 ? 388 GLU A CD  1 
ATOM   2538 O  OE1 . GLU A 1 388 ? 1.599   9.812   -3.868  1.00 39.66 ? 388 GLU A OE1 1 
ATOM   2539 O  OE2 . GLU A 1 388 ? -0.030  10.247  -2.402  1.00 62.52 ? 388 GLU A OE2 1 
ATOM   2540 N  N   . PHE A 1 389 ? 3.745   6.405   -0.303  1.00 14.31 ? 389 PHE A N   1 
ATOM   2541 C  CA  . PHE A 1 389 ? 3.456   6.114   1.095   1.00 14.04 ? 389 PHE A CA  1 
ATOM   2542 C  C   . PHE A 1 389 ? 4.733   6.111   1.916   1.00 13.02 ? 389 PHE A C   1 
ATOM   2543 O  O   . PHE A 1 389 ? 4.642   5.838   3.095   1.00 15.92 ? 389 PHE A O   1 
ATOM   2544 C  CB  . PHE A 1 389 ? 2.768   4.757   1.258   1.00 12.59 ? 389 PHE A CB  1 
ATOM   2545 C  CG  . PHE A 1 389 ? 1.489   4.674   0.484   1.00 13.11 ? 389 PHE A CG  1 
ATOM   2546 C  CD1 . PHE A 1 389 ? 0.365   5.338   0.970   1.00 14.99 ? 389 PHE A CD1 1 
ATOM   2547 C  CD2 . PHE A 1 389 ? 1.397   3.996   -0.720  1.00 15.02 ? 389 PHE A CD2 1 
ATOM   2548 C  CE1 . PHE A 1 389 ? -0.835  5.283   0.291   1.00 14.96 ? 389 PHE A CE1 1 
ATOM   2549 C  CE2 . PHE A 1 389 ? 0.204   3.977   -1.436  1.00 16.15 ? 389 PHE A CE2 1 
ATOM   2550 C  CZ  . PHE A 1 389 ? -0.904  4.602   -0.915  1.00 14.94 ? 389 PHE A CZ  1 
ATOM   2551 N  N   . ILE A 1 390 ? 5.875   6.424   1.329   1.00 12.99 ? 390 ILE A N   1 
ATOM   2552 C  CA  . ILE A 1 390 ? 7.145   6.318   2.065   1.00 14.05 ? 390 ILE A CA  1 
ATOM   2553 C  C   . ILE A 1 390 ? 8.001   7.515   1.736   1.00 15.59 ? 390 ILE A C   1 
ATOM   2554 O  O   . ILE A 1 390 ? 7.804   8.167   0.705   1.00 15.29 ? 390 ILE A O   1 
ATOM   2555 C  CB  . ILE A 1 390 ? 7.873   4.997   1.753   1.00 14.21 ? 390 ILE A CB  1 
ATOM   2556 C  CG1 . ILE A 1 390 ? 8.296   4.887   0.277   1.00 14.99 ? 390 ILE A CG1 1 
ATOM   2557 C  CG2 . ILE A 1 390 ? 7.031   3.794   2.195   1.00 15.13 ? 390 ILE A CG2 1 
ATOM   2558 C  CD1 . ILE A 1 390 ? 9.316   3.842   -0.051  1.00 16.62 ? 390 ILE A CD1 1 
ATOM   2559 N  N   . GLN A 1 391 ? 9.056   7.727   2.558   1.00 14.84 ? 391 GLN A N   1 
ATOM   2560 C  CA  . GLN A 1 391 ? 10.059  8.715   2.255   1.00 15.21 ? 391 GLN A CA  1 
ATOM   2561 C  C   . GLN A 1 391 ? 11.342  8.231   2.884   1.00 14.87 ? 391 GLN A C   1 
ATOM   2562 O  O   . GLN A 1 391 ? 11.320  7.956   4.076   1.00 16.38 ? 391 GLN A O   1 
ATOM   2563 C  CB  . GLN A 1 391 ? 9.681   10.114  2.760   1.00 16.34 ? 391 GLN A CB  1 
ATOM   2564 C  CG  . GLN A 1 391 ? 10.597  11.182  2.152   1.00 20.25 ? 391 GLN A CG  1 
ATOM   2565 C  CD  . GLN A 1 391 ? 10.301  12.546  2.708   1.00 24.65 ? 391 GLN A CD  1 
ATOM   2566 O  OE1 . GLN A 1 391 ? 10.250  12.779  3.914   1.00 30.39 ? 391 GLN A OE1 1 
ATOM   2567 N  NE2 . GLN A 1 391 ? 10.029  13.450  1.787   1.00 32.28 ? 391 GLN A NE2 1 
ATOM   2568 N  N   . HIS A 1 392 ? 12.407  8.199   2.083   1.00 14.25 ? 392 HIS A N   1 
ATOM   2569 C  CA  . HIS A 1 392 ? 13.718  7.859   2.593   1.00 14.56 ? 392 HIS A CA  1 
ATOM   2570 C  C   . HIS A 1 392 ? 14.284  9.100   3.268   1.00 15.90 ? 392 HIS A C   1 
ATOM   2571 O  O   . HIS A 1 392 ? 14.420  10.124  2.600   1.00 17.07 ? 392 HIS A O   1 
ATOM   2572 C  CB  . HIS A 1 392 ? 14.665  7.397   1.494   1.00 16.53 ? 392 HIS A CB  1 
ATOM   2573 C  CG  . HIS A 1 392 ? 14.305  6.101   0.847   1.00 16.30 ? 392 HIS A CG  1 
ATOM   2574 N  ND1 . HIS A 1 392 ? 15.164  5.015   0.804   1.00 17.62 ? 392 HIS A ND1 1 
ATOM   2575 C  CD2 . HIS A 1 392 ? 13.149  5.697   0.251   1.00 16.26 ? 392 HIS A CD2 1 
ATOM   2576 C  CE1 . HIS A 1 392 ? 14.561  4.034   0.140   1.00 17.41 ? 392 HIS A CE1 1 
ATOM   2577 N  NE2 . HIS A 1 392 ? 13.303  4.423   -0.222  1.00 17.07 ? 392 HIS A NE2 1 
ATOM   2578 N  N   . VAL A 1 393 ? 14.567  9.002   4.572   1.00 14.86 ? 393 VAL A N   1 
ATOM   2579 C  CA  . VAL A 1 393 ? 15.067  10.142  5.335   1.00 16.76 ? 393 VAL A CA  1 
ATOM   2580 C  C   . VAL A 1 393 ? 16.452  9.939   5.995   1.00 18.24 ? 393 VAL A C   1 
ATOM   2581 O  O   . VAL A 1 393 ? 16.925  10.821  6.697   1.00 17.06 ? 393 VAL A O   1 
ATOM   2582 C  CB  . VAL A 1 393 ? 14.003  10.525  6.380   1.00 17.93 ? 393 VAL A CB  1 
ATOM   2583 C  CG1 . VAL A 1 393 ? 12.693  10.941  5.732   1.00 19.28 ? 393 VAL A CG1 1 
ATOM   2584 C  CG2 . VAL A 1 393 ? 13.752  9.393   7.346   1.00 19.04 ? 393 VAL A CG2 1 
ATOM   2585 N  N   . GLY A 1 394 ? 17.131  8.817   5.742   1.00 15.42 ? 394 GLY A N   1 
ATOM   2586 C  CA  . GLY A 1 394 ? 18.461  8.561   6.285   1.00 14.58 ? 394 GLY A CA  1 
ATOM   2587 C  C   . GLY A 1 394 ? 19.148  7.518   5.416   1.00 13.30 ? 394 GLY A C   1 
ATOM   2588 O  O   . GLY A 1 394 ? 18.432  6.684   4.871   1.00 17.51 ? 394 GLY A O   1 
ATOM   2589 N  N   . SER A 1 395 ? 20.467  7.577   5.253   1.00 13.80 ? 395 SER A N   1 
ATOM   2590 C  CA  . SER A 1 395 ? 21.169  6.653   4.394   1.00 15.71 ? 395 SER A CA  1 
ATOM   2591 C  C   . SER A 1 395 ? 22.606  6.478   4.862   1.00 16.35 ? 395 SER A C   1 
ATOM   2592 O  O   . SER A 1 395 ? 23.229  7.427   5.315   1.00 17.02 ? 395 SER A O   1 
ATOM   2593 C  CB  . SER A 1 395 ? 21.078  7.132   2.973   1.00 17.62 ? 395 SER A CB  1 
ATOM   2594 O  OG  . SER A 1 395 ? 21.765  6.285   2.088   1.00 18.83 ? 395 SER A OG  1 
ATOM   2595 N  N   . ALA A 1 396 ? 23.148  5.253   4.709   1.00 15.70 ? 396 ALA A N   1 
ATOM   2596 C  CA  . ALA A 1 396 ? 24.550  4.989   4.962   1.00 15.28 ? 396 ALA A CA  1 
ATOM   2597 C  C   . ALA A 1 396 ? 24.943  3.694   4.295   1.00 17.38 ? 396 ALA A C   1 
ATOM   2598 O  O   . ALA A 1 396 ? 24.085  2.838   4.107   1.00 18.46 ? 396 ALA A O   1 
ATOM   2599 C  CB  . ALA A 1 396 ? 24.797  4.917   6.469   1.00 17.80 ? 396 ALA A CB  1 
ATOM   2600 N  N   . VAL A 1 397 ? 26.189  3.641   3.837   1.00 15.94 ? 397 VAL A N   1 
ATOM   2601 C  CA  . VAL A 1 397 ? 26.780  2.444   3.311   1.00 16.46 ? 397 VAL A CA  1 
ATOM   2602 C  C   . VAL A 1 397 ? 28.040  2.092   4.114   1.00 14.19 ? 397 VAL A C   1 
ATOM   2603 O  O   . VAL A 1 397 ? 28.742  2.959   4.652   1.00 14.90 ? 397 VAL A O   1 
ATOM   2604 C  CB  . VAL A 1 397 ? 27.104  2.557   1.813   1.00 16.61 ? 397 VAL A CB  1 
ATOM   2605 C  CG1 . VAL A 1 397 ? 25.859  2.871   1.003   1.00 19.29 ? 397 VAL A CG1 1 
ATOM   2606 C  CG2 . VAL A 1 397 ? 28.194  3.563   1.509   1.00 19.41 ? 397 VAL A CG2 1 
ATOM   2607 N  N   . PHE A 1 398 ? 28.251  0.797   4.223   1.00 14.78 ? 398 PHE A N   1 
ATOM   2608 C  CA  . PHE A 1 398 ? 29.349  0.224   4.981   1.00 15.91 ? 398 PHE A CA  1 
ATOM   2609 C  C   . PHE A 1 398 ? 29.895  -1.005  4.273   1.00 17.39 ? 398 PHE A C   1 
ATOM   2610 O  O   . PHE A 1 398 ? 29.148  -1.819  3.715   1.00 17.20 ? 398 PHE A O   1 
ATOM   2611 C  CB  . PHE A 1 398 ? 28.926  -0.145  6.397   1.00 14.91 ? 398 PHE A CB  1 
ATOM   2612 C  CG  . PHE A 1 398 ? 28.330  0.978   7.174   1.00 15.01 ? 398 PHE A CG  1 
ATOM   2613 C  CD1 . PHE A 1 398 ? 29.163  1.894   7.815   1.00 16.10 ? 398 PHE A CD1 1 
ATOM   2614 C  CD2 . PHE A 1 398 ? 26.960  1.134   7.234   1.00 16.65 ? 398 PHE A CD2 1 
ATOM   2615 C  CE1 . PHE A 1 398 ? 28.595  2.952   8.508   1.00 17.15 ? 398 PHE A CE1 1 
ATOM   2616 C  CE2 . PHE A 1 398 ? 26.401  2.159   7.965   1.00 16.07 ? 398 PHE A CE2 1 
ATOM   2617 C  CZ  . PHE A 1 398 ? 27.219  3.072   8.585   1.00 16.30 ? 398 PHE A CZ  1 
ATOM   2618 N  N   . ALA A 1 399 ? 31.232  -1.136  4.344   1.00 15.06 ? 399 ALA A N   1 
ATOM   2619 C  CA  . ALA A 1 399 ? 31.918  -2.369  4.028   1.00 15.92 ? 399 ALA A CA  1 
ATOM   2620 C  C   . ALA A 1 399 ? 32.007  -3.184  5.308   1.00 13.02 ? 399 ALA A C   1 
ATOM   2621 O  O   . ALA A 1 399 ? 32.606  -2.737  6.292   1.00 16.95 ? 399 ALA A O   1 
ATOM   2622 C  CB  . ALA A 1 399 ? 33.314  -2.111  3.486   1.00 14.48 ? 399 ALA A CB  1 
ATOM   2623 N  N   . VAL A 1 400 ? 31.414  -4.353  5.258   1.00 14.65 ? 400 VAL A N   1 
ATOM   2624 C  CA  . VAL A 1 400 ? 31.341  -5.284  6.361   1.00 14.67 ? 400 VAL A CA  1 
ATOM   2625 C  C   . VAL A 1 400 ? 32.463  -6.270  6.192   1.00 13.95 ? 400 VAL A C   1 
ATOM   2626 O  O   . VAL A 1 400 ? 32.432  -7.111  5.303   1.00 14.62 ? 400 VAL A O   1 
ATOM   2627 C  CB  . VAL A 1 400 ? 29.963  -5.948  6.402   1.00 16.22 ? 400 VAL A CB  1 
ATOM   2628 C  CG1 . VAL A 1 400 ? 29.856  -6.942  7.531   1.00 19.41 ? 400 VAL A CG1 1 
ATOM   2629 C  CG2 . VAL A 1 400 ? 28.871  -4.878  6.578   1.00 19.26 ? 400 VAL A CG2 1 
ATOM   2630 N  N   . PRO A 1 401 ? 33.554  -6.182  6.998   1.00 15.28 ? 401 PRO A N   1 
ATOM   2631 C  CA  . PRO A 1 401 ? 34.684  -7.077  6.727   1.00 16.08 ? 401 PRO A CA  1 
ATOM   2632 C  C   . PRO A 1 401 ? 34.359  -8.554  6.918   1.00 17.16 ? 401 PRO A C   1 
ATOM   2633 O  O   . PRO A 1 401 ? 33.329  -8.967  7.470   1.00 16.82 ? 401 PRO A O   1 
ATOM   2634 C  CB  . PRO A 1 401 ? 35.768  -6.582  7.696   1.00 15.95 ? 401 PRO A CB  1 
ATOM   2635 C  CG  . PRO A 1 401 ? 35.016  -5.869  8.776   1.00 17.91 ? 401 PRO A CG  1 
ATOM   2636 C  CD  . PRO A 1 401 ? 33.786  -5.238  8.083   1.00 15.07 ? 401 PRO A CD  1 
ATOM   2637 N  N   . PRO A 1 402 ? 35.317  -9.442  6.577   1.00 15.29 ? 402 PRO A N   1 
ATOM   2638 C  CA  . PRO A 1 402 ? 35.199  -10.870 6.841   1.00 17.19 ? 402 PRO A CA  1 
ATOM   2639 C  C   . PRO A 1 402 ? 35.123  -11.162 8.326   1.00 17.61 ? 402 PRO A C   1 
ATOM   2640 O  O   . PRO A 1 402 ? 35.404  -10.285 9.160   1.00 16.55 ? 402 PRO A O   1 
ATOM   2641 C  CB  . PRO A 1 402 ? 36.479  -11.522 6.274   1.00 20.09 ? 402 PRO A CB  1 
ATOM   2642 C  CG  . PRO A 1 402 ? 37.249  -10.415 5.693   1.00 18.91 ? 402 PRO A CG  1 
ATOM   2643 C  CD  . PRO A 1 402 ? 36.609  -9.089  5.968   1.00 19.31 ? 402 PRO A CD  1 
ATOM   2644 N  N   . GLY A 1 403 ? 34.847  -12.425 8.591   1.00 15.44 ? 403 GLY A N   1 
ATOM   2645 C  CA  . GLY A 1 403 ? 34.667  -12.932 9.924   1.00 18.34 ? 403 GLY A CA  1 
ATOM   2646 C  C   . GLY A 1 403 ? 35.968  -12.957 10.745  1.00 18.66 ? 403 GLY A C   1 
ATOM   2647 O  O   . GLY A 1 403 ? 37.062  -12.867 10.217  1.00 20.26 ? 403 GLY A O   1 
ATOM   2648 N  N   . VAL A 1 404 ? 35.758  -13.106 12.020  1.00 16.24 ? 404 VAL A N   1 
ATOM   2649 C  CA  . VAL A 1 404 ? 36.813  -13.248 13.006  1.00 17.75 ? 404 VAL A CA  1 
ATOM   2650 C  C   . VAL A 1 404 ? 37.091  -14.743 13.052  1.00 16.43 ? 404 VAL A C   1 
ATOM   2651 O  O   . VAL A 1 404 ? 36.261  -15.508 13.473  1.00 16.23 ? 404 VAL A O   1 
ATOM   2652 C  CB  . VAL A 1 404 ? 36.385  -12.675 14.374  1.00 19.46 ? 404 VAL A CB  1 
ATOM   2653 C  CG1 . VAL A 1 404 ? 37.529  -12.843 15.385  1.00 19.65 ? 404 VAL A CG1 1 
ATOM   2654 C  CG2 . VAL A 1 404 ? 35.910  -11.225 14.287  1.00 21.07 ? 404 VAL A CG2 1 
ATOM   2655 N  N   . ARG A 1 405 ? 38.264  -15.172 12.600  1.00 18.04 ? 405 ARG A N   1 
ATOM   2656 C  CA  . ARG A 1 405 ? 38.488  -16.567 12.244  1.00 21.60 ? 405 ARG A CA  1 
ATOM   2657 C  C   . ARG A 1 405 ? 38.570  -17.421 13.513  1.00 20.23 ? 405 ARG A C   1 
ATOM   2658 O  O   . ARG A 1 405 ? 38.054  -18.555 13.594  1.00 21.63 ? 405 ARG A O   1 
ATOM   2659 C  CB  . ARG A 1 405 ? 39.754  -16.702 11.374  1.00 23.63 ? 405 ARG A CB  1 
ATOM   2660 C  CG  . ARG A 1 405 ? 39.679  -16.070 9.987   1.00 35.17 ? 405 ARG A CG  1 
ATOM   2661 N  N   . ASP A 1 406 ? 39.223  -16.865 14.538  1.00 20.01 ? 406 ASP A N   1 
ATOM   2662 C  CA  . ASP A 1 406 ? 39.483  -17.600 15.756  1.00 22.34 ? 406 ASP A CA  1 
ATOM   2663 C  C   . ASP A 1 406 ? 39.821  -16.597 16.853  1.00 20.62 ? 406 ASP A C   1 
ATOM   2664 O  O   . ASP A 1 406 ? 39.787  -15.383 16.658  1.00 16.80 ? 406 ASP A O   1 
ATOM   2665 C  CB  . ASP A 1 406 ? 40.612  -18.590 15.441  1.00 20.81 ? 406 ASP A CB  1 
ATOM   2666 C  CG  . ASP A 1 406 ? 41.889  -17.879 15.034  1.00 21.43 ? 406 ASP A CG  1 
ATOM   2667 O  OD1 . ASP A 1 406 ? 42.205  -16.830 15.577  1.00 22.42 ? 406 ASP A OD1 1 
ATOM   2668 O  OD2 . ASP A 1 406 ? 42.552  -18.423 14.183  1.00 41.87 ? 406 ASP A OD2 1 
ATOM   2669 N  N   . ALA A 1 407 ? 40.211  -17.084 18.048  1.00 21.41 ? 407 ALA A N   1 
ATOM   2670 C  CA  . ALA A 1 407 ? 40.368  -16.262 19.241  1.00 21.30 ? 407 ALA A CA  1 
ATOM   2671 C  C   . ALA A 1 407 ? 41.544  -15.295 19.162  1.00 20.13 ? 407 ALA A C   1 
ATOM   2672 O  O   . ALA A 1 407 ? 41.658  -14.360 19.930  1.00 22.81 ? 407 ALA A O   1 
ATOM   2673 C  CB  . ALA A 1 407 ? 40.495  -17.146 20.472  1.00 21.37 ? 407 ALA A CB  1 
ATOM   2674 N  N   . ASP A 1 408 ? 42.432  -15.487 18.218  1.00 22.74 ? 408 ASP A N   1 
ATOM   2675 C  CA  . ASP A 1 408 ? 43.581  -14.619 18.009  1.00 25.15 ? 408 ASP A CA  1 
ATOM   2676 C  C   . ASP A 1 408 ? 43.360  -13.577 16.909  1.00 23.48 ? 408 ASP A C   1 
ATOM   2677 O  O   . ASP A 1 408 ? 44.104  -12.618 16.790  1.00 25.17 ? 408 ASP A O   1 
ATOM   2678 C  CB  . ASP A 1 408 ? 44.751  -15.506 17.564  1.00 32.15 ? 408 ASP A CB  1 
ATOM   2679 C  CG  . ASP A 1 408 ? 45.675  -15.786 18.724  1.00 42.11 ? 408 ASP A CG  1 
ATOM   2680 O  OD1 . ASP A 1 408 ? 46.197  -14.772 19.252  1.00 49.49 ? 408 ASP A OD1 1 
ATOM   2681 O  OD2 . ASP A 1 408 ? 45.792  -16.966 19.131  1.00 61.56 ? 408 ASP A OD2 1 
ATOM   2682 N  N   . ASP A 1 409 ? 42.237  -13.660 16.209  1.00 20.02 ? 409 ASP A N   1 
ATOM   2683 C  CA  . ASP A 1 409 ? 41.901  -12.679 15.193  1.00 18.43 ? 409 ASP A CA  1 
ATOM   2684 C  C   . ASP A 1 409 ? 41.131  -11.517 15.812  1.00 20.89 ? 409 ASP A C   1 
ATOM   2685 O  O   . ASP A 1 409 ? 40.770  -11.519 16.965  1.00 20.41 ? 409 ASP A O   1 
ATOM   2686 C  CB  . ASP A 1 409 ? 41.114  -13.400 14.085  1.00 19.52 ? 409 ASP A CB  1 
ATOM   2687 C  CG  . ASP A 1 409 ? 41.043  -12.650 12.763  1.00 21.56 ? 409 ASP A CG  1 
ATOM   2688 O  OD1 . ASP A 1 409 ? 41.776  -11.698 12.600  1.00 22.41 ? 409 ASP A OD1 1 
ATOM   2689 O  OD2 . ASP A 1 409 ? 40.277  -13.056 11.903  1.00 23.88 ? 409 ASP A OD2 1 
ATOM   2690 N  N   . TRP A 1 410 ? 40.856  -10.478 14.984  1.00 18.56 ? 410 TRP A N   1 
ATOM   2691 C  CA  . TRP A 1 410 ? 40.200  -9.281  15.475  1.00 19.95 ? 410 TRP A CA  1 
ATOM   2692 C  C   . TRP A 1 410 ? 39.516  -8.618  14.291  1.00 16.59 ? 410 TRP A C   1 
ATOM   2693 O  O   . TRP A 1 410 ? 39.945  -8.739  13.161  1.00 16.99 ? 410 TRP A O   1 
ATOM   2694 C  CB  . TRP A 1 410 ? 41.162  -8.363  16.259  1.00 19.23 ? 410 TRP A CB  1 
ATOM   2695 C  CG  . TRP A 1 410 ? 42.528  -8.186  15.633  1.00 19.94 ? 410 TRP A CG  1 
ATOM   2696 C  CD1 . TRP A 1 410 ? 43.618  -9.023  15.703  1.00 21.33 ? 410 TRP A CD1 1 
ATOM   2697 C  CD2 . TRP A 1 410 ? 42.933  -7.053  14.841  1.00 21.58 ? 410 TRP A CD2 1 
ATOM   2698 N  NE1 . TRP A 1 410 ? 44.668  -8.478  14.991  1.00 24.03 ? 410 TRP A NE1 1 
ATOM   2699 C  CE2 . TRP A 1 410 ? 44.277  -7.270  14.465  1.00 24.19 ? 410 TRP A CE2 1 
ATOM   2700 C  CE3 . TRP A 1 410 ? 42.296  -5.870  14.418  1.00 22.68 ? 410 TRP A CE3 1 
ATOM   2701 C  CZ2 . TRP A 1 410 ? 44.980  -6.317  13.727  1.00 22.55 ? 410 TRP A CZ2 1 
ATOM   2702 C  CZ3 . TRP A 1 410 ? 42.989  -4.953  13.666  1.00 22.68 ? 410 TRP A CZ3 1 
ATOM   2703 C  CH2 . TRP A 1 410 ? 44.299  -5.213  13.300  1.00 21.84 ? 410 TRP A CH2 1 
ATOM   2704 N  N   . TRP A 1 411 ? 38.430  -7.926  14.605  1.00 16.80 ? 411 TRP A N   1 
ATOM   2705 C  CA  . TRP A 1 411 ? 37.689  -7.109  13.665  1.00 16.66 ? 411 TRP A CA  1 
ATOM   2706 C  C   . TRP A 1 411 ? 38.617  -6.191  12.855  1.00 18.00 ? 411 TRP A C   1 
ATOM   2707 O  O   . TRP A 1 411 ? 39.310  -5.384  13.459  1.00 17.58 ? 411 TRP A O   1 
ATOM   2708 C  CB  . TRP A 1 411 ? 36.726  -6.244  14.480  1.00 16.10 ? 411 TRP A CB  1 
ATOM   2709 C  CG  . TRP A 1 411 ? 35.436  -6.900  14.797  1.00 14.62 ? 411 TRP A CG  1 
ATOM   2710 C  CD1 . TRP A 1 411 ? 34.899  -7.991  14.191  1.00 15.32 ? 411 TRP A CD1 1 
ATOM   2711 C  CD2 . TRP A 1 411 ? 34.486  -6.449  15.762  1.00 13.08 ? 411 TRP A CD2 1 
ATOM   2712 N  NE1 . TRP A 1 411 ? 33.645  -8.219  14.689  1.00 15.90 ? 411 TRP A NE1 1 
ATOM   2713 C  CE2 . TRP A 1 411 ? 33.372  -7.301  15.660  1.00 15.34 ? 411 TRP A CE2 1 
ATOM   2714 C  CE3 . TRP A 1 411 ? 34.442  -5.379  16.650  1.00 17.37 ? 411 TRP A CE3 1 
ATOM   2715 C  CZ2 . TRP A 1 411 ? 32.242  -7.153  16.466  1.00 16.07 ? 411 TRP A CZ2 1 
ATOM   2716 C  CZ3 . TRP A 1 411 ? 33.293  -5.213  17.439  1.00 20.48 ? 411 TRP A CZ3 1 
ATOM   2717 C  CH2 . TRP A 1 411 ? 32.209  -6.069  17.309  1.00 16.94 ? 411 TRP A CH2 1 
ATOM   2718 N  N   . GLY A 1 412 ? 38.561  -6.296  11.521  1.00 18.01 ? 412 GLY A N   1 
ATOM   2719 C  CA  . GLY A 1 412 ? 39.340  -5.374  10.712  1.00 18.68 ? 412 GLY A CA  1 
ATOM   2720 C  C   . GLY A 1 412 ? 40.788  -5.793  10.482  1.00 20.20 ? 412 GLY A C   1 
ATOM   2721 O  O   . GLY A 1 412 ? 41.511  -5.065  9.808   1.00 20.62 ? 412 GLY A O   1 
ATOM   2722 N  N   . SER A 1 413 ? 41.178  -7.002  10.943  1.00 18.44 ? 413 SER A N   1 
ATOM   2723 C  CA  . SER A 1 413 ? 42.548  -7.456  10.870  1.00 19.26 ? 413 SER A CA  1 
ATOM   2724 C  C   . SER A 1 413 ? 43.016  -7.544  9.426   1.00 18.48 ? 413 SER A C   1 
ATOM   2725 O  O   . SER A 1 413 ? 44.190  -7.345  9.167   1.00 23.61 ? 413 SER A O   1 
ATOM   2726 C  CB  . SER A 1 413 ? 42.713  -8.793  11.539  1.00 17.21 ? 413 SER A CB  1 
ATOM   2727 O  OG  . SER A 1 413 ? 42.048  -9.812  10.781  1.00 17.19 ? 413 SER A OG  1 
ATOM   2728 N  N   . THR A 1 414 ? 42.117  -7.870  8.495   1.00 21.94 ? 414 THR A N   1 
ATOM   2729 C  CA  . THR A 1 414 ? 42.530  -8.036  7.116   1.00 19.47 ? 414 THR A CA  1 
ATOM   2730 C  C   . THR A 1 414 ? 42.768  -6.662  6.493   1.00 20.67 ? 414 THR A C   1 
ATOM   2731 O  O   . THR A 1 414 ? 43.458  -6.582  5.488   1.00 23.69 ? 414 THR A O   1 
ATOM   2732 C  CB  . THR A 1 414 ? 41.555  -8.855  6.241   1.00 22.24 ? 414 THR A CB  1 
ATOM   2733 O  OG1 . THR A 1 414 ? 40.333  -8.133  6.187   1.00 19.80 ? 414 THR A OG1 1 
ATOM   2734 C  CG2 . THR A 1 414 ? 41.349  -10.258 6.735   1.00 24.37 ? 414 THR A CG2 1 
ATOM   2735 N  N   . LEU A 1 415 ? 42.165  -5.597  7.013   1.00 20.67 ? 415 LEU A N   1 
ATOM   2736 C  CA  . LEU A 1 415 ? 42.385  -4.256  6.489   1.00 24.43 ? 415 LEU A CA  1 
ATOM   2737 C  C   . LEU A 1 415 ? 43.633  -3.649  7.128   1.00 27.53 ? 415 LEU A C   1 
ATOM   2738 O  O   . LEU A 1 415 ? 44.418  -3.014  6.428   1.00 27.70 ? 415 LEU A O   1 
ATOM   2739 C  CB  . LEU A 1 415 ? 41.172  -3.371  6.790   1.00 24.57 ? 415 LEU A CB  1 
ATOM   2740 C  CG  . LEU A 1 415 ? 41.305  -1.898  6.376   1.00 27.49 ? 415 LEU A CG  1 
ATOM   2741 C  CD1 . LEU A 1 415 ? 41.625  -1.732  4.892   1.00 28.40 ? 415 LEU A CD1 1 
ATOM   2742 C  CD2 . LEU A 1 415 ? 40.031  -1.165  6.772   1.00 27.97 ? 415 LEU A CD2 1 
ATOM   2743 N  N   . PHE A 1 416 ? 43.739  -3.766  8.457   1.00 23.56 ? 416 PHE A N   1 
ATOM   2744 C  CA  . PHE A 1 416 ? 44.838  -3.212  9.220   1.00 26.75 ? 416 PHE A CA  1 
ATOM   2745 C  C   . PHE A 1 416 ? 45.970  -4.248  9.299   1.00 28.85 ? 416 PHE A C   1 
ATOM   2746 O  O   . PHE A 1 416 ? 47.049  -3.636  9.296   1.00 36.18 ? 416 PHE A O   1 
ATOM   2747 C  CB  . PHE A 1 416 ? 44.317  -2.677  10.547  1.00 25.11 ? 416 PHE A CB  1 
ATOM   2748 C  CG  . PHE A 1 416 ? 43.373  -1.501  10.446  1.00 26.73 ? 416 PHE A CG  1 
ATOM   2749 C  CD1 . PHE A 1 416 ? 43.826  -0.180  10.431  1.00 30.44 ? 416 PHE A CD1 1 
ATOM   2750 C  CD2 . PHE A 1 416 ? 41.993  -1.692  10.385  1.00 27.15 ? 416 PHE A CD2 1 
ATOM   2751 C  CE1 . PHE A 1 416 ? 42.941  0.889   10.348  1.00 30.21 ? 416 PHE A CE1 1 
ATOM   2752 C  CE2 . PHE A 1 416 ? 41.117  -0.615  10.345  1.00 26.79 ? 416 PHE A CE2 1 
ATOM   2753 C  CZ  . PHE A 1 416 ? 41.596  0.675   10.340  1.00 28.69 ? 416 PHE A CZ  1 
ATOM   2754 N  N   . SER B 1 56  ? -1.087  -16.970 28.013  1.00 43.19 ? 56  SER B N   1 
ATOM   2755 C  CA  . SER B 1 56  ? -1.182  -16.361 26.652  1.00 37.06 ? 56  SER B CA  1 
ATOM   2756 C  C   . SER B 1 56  ? -2.191  -15.189 26.613  1.00 26.65 ? 56  SER B C   1 
ATOM   2757 O  O   . SER B 1 56  ? -1.867  -14.279 25.938  1.00 24.56 ? 56  SER B O   1 
ATOM   2758 C  CB  . SER B 1 56  ? -1.325  -17.380 25.537  1.00 43.40 ? 56  SER B CB  1 
ATOM   2759 O  OG  . SER B 1 56  ? -2.637  -17.435 24.989  1.00 52.37 ? 56  SER B OG  1 
ATOM   2760 N  N   . ALA B 1 57  ? -3.315  -15.136 27.346  1.00 26.56 ? 57  ALA B N   1 
ATOM   2761 C  CA  . ALA B 1 57  ? -4.196  -13.960 27.347  1.00 21.52 ? 57  ALA B CA  1 
ATOM   2762 C  C   . ALA B 1 57  ? -4.561  -13.615 28.788  1.00 21.41 ? 57  ALA B C   1 
ATOM   2763 O  O   . ALA B 1 57  ? -4.404  -14.442 29.682  1.00 22.68 ? 57  ALA B O   1 
ATOM   2764 C  CB  . ALA B 1 57  ? -5.405  -14.222 26.469  1.00 22.58 ? 57  ALA B CB  1 
ATOM   2765 N  N   . VAL B 1 58  ? -4.875  -12.345 29.035  1.00 14.67 ? 58  VAL B N   1 
ATOM   2766 C  CA  . VAL B 1 58  ? -5.277  -11.831 30.310  1.00 13.85 ? 58  VAL B CA  1 
ATOM   2767 C  C   . VAL B 1 58  ? -6.711  -11.403 30.127  1.00 12.90 ? 58  VAL B C   1 
ATOM   2768 O  O   . VAL B 1 58  ? -7.088  -10.720 29.163  1.00 12.94 ? 58  VAL B O   1 
ATOM   2769 C  CB  . VAL B 1 58  ? -4.344  -10.687 30.766  1.00 15.12 ? 58  VAL B CB  1 
ATOM   2770 C  CG1 . VAL B 1 58  ? -4.900  -10.032 32.035  1.00 16.33 ? 58  VAL B CG1 1 
ATOM   2771 C  CG2 . VAL B 1 58  ? -2.932  -11.179 30.950  1.00 16.72 ? 58  VAL B CG2 1 
ATOM   2772 N  N   . PRO B 1 59  ? -7.633  -11.835 30.998  1.00 14.17 ? 59  PRO B N   1 
ATOM   2773 C  CA  . PRO B 1 59  ? -9.035  -11.450 30.818  1.00 14.17 ? 59  PRO B CA  1 
ATOM   2774 C  C   . PRO B 1 59  ? -9.186  -9.912  30.834  1.00 15.08 ? 59  PRO B C   1 
ATOM   2775 O  O   . PRO B 1 59  ? -8.614  -9.198  31.662  1.00 15.57 ? 59  PRO B O   1 
ATOM   2776 C  CB  . PRO B 1 59  ? -9.768  -12.094 32.024  1.00 17.51 ? 59  PRO B CB  1 
ATOM   2777 C  CG  . PRO B 1 59  ? -8.788  -13.033 32.646  1.00 17.95 ? 59  PRO B CG  1 
ATOM   2778 C  CD  . PRO B 1 59  ? -7.372  -12.707 32.159  1.00 18.49 ? 59  PRO B CD  1 
ATOM   2779 N  N   . PHE B 1 60  ? -10.013 -9.406  29.923  1.00 15.16 ? 60  PHE B N   1 
ATOM   2780 C  CA  . PHE B 1 60  ? -10.268 -7.983  29.771  1.00 17.97 ? 60  PHE B CA  1 
ATOM   2781 C  C   . PHE B 1 60  ? -11.242 -7.488  30.870  1.00 14.36 ? 60  PHE B C   1 
ATOM   2782 O  O   . PHE B 1 60  ? -11.114 -6.371  31.383  1.00 12.05 ? 60  PHE B O   1 
ATOM   2783 C  CB  . PHE B 1 60  ? -10.765 -7.734  28.335  1.00 16.95 ? 60  PHE B CB  1 
ATOM   2784 C  CG  . PHE B 1 60  ? -11.104 -6.298  28.052  1.00 16.25 ? 60  PHE B CG  1 
ATOM   2785 C  CD1 . PHE B 1 60  ? -10.092 -5.342  27.992  1.00 17.53 ? 60  PHE B CD1 1 
ATOM   2786 C  CD2 . PHE B 1 60  ? -12.417 -5.861  27.966  1.00 17.13 ? 60  PHE B CD2 1 
ATOM   2787 C  CE1 . PHE B 1 60  ? -10.379 -3.988  27.840  1.00 16.69 ? 60  PHE B CE1 1 
ATOM   2788 C  CE2 . PHE B 1 60  ? -12.684 -4.521  27.753  1.00 18.98 ? 60  PHE B CE2 1 
ATOM   2789 C  CZ  . PHE B 1 60  ? -11.669 -3.597  27.699  1.00 15.68 ? 60  PHE B CZ  1 
ATOM   2790 N  N   . HIS B 1 61  ? -12.297 -8.279  31.159  1.00 15.78 ? 61  HIS B N   1 
ATOM   2791 C  CA  . HIS B 1 61  ? -13.369 -7.889  32.061  1.00 17.52 ? 61  HIS B CA  1 
ATOM   2792 C  C   . HIS B 1 61  ? -12.974 -8.141  33.491  1.00 16.64 ? 61  HIS B C   1 
ATOM   2793 O  O   . HIS B 1 61  ? -12.307 -9.117  33.812  1.00 19.77 ? 61  HIS B O   1 
ATOM   2794 C  CB  . HIS B 1 61  ? -14.667 -8.657  31.752  1.00 16.68 ? 61  HIS B CB  1 
ATOM   2795 C  CG  . HIS B 1 61  ? -15.153 -8.403  30.372  1.00 18.18 ? 61  HIS B CG  1 
ATOM   2796 N  ND1 . HIS B 1 61  ? -15.052 -9.317  29.352  1.00 22.25 ? 61  HIS B ND1 1 
ATOM   2797 C  CD2 . HIS B 1 61  ? -15.588 -7.219  29.810  1.00 19.54 ? 61  HIS B CD2 1 
ATOM   2798 C  CE1 . HIS B 1 61  ? -15.480 -8.723  28.228  1.00 25.83 ? 61  HIS B CE1 1 
ATOM   2799 N  NE2 . HIS B 1 61  ? -15.950 -7.479  28.516  1.00 22.76 ? 61  HIS B NE2 1 
ATOM   2800 N  N   . GLY B 1 62  ? -13.499 -7.284  34.365  1.00 16.04 ? 62  GLY B N   1 
ATOM   2801 C  CA  . GLY B 1 62  ? -13.380 -7.475  35.778  1.00 19.85 ? 62  GLY B CA  1 
ATOM   2802 C  C   . GLY B 1 62  ? -13.835 -6.237  36.532  1.00 15.59 ? 62  GLY B C   1 
ATOM   2803 O  O   . GLY B 1 62  ? -14.212 -5.240  35.950  1.00 16.60 ? 62  GLY B O   1 
ATOM   2804 N  N   . ALA B 1 63  ? -13.712 -6.318  37.860  1.00 16.45 ? 63  ALA B N   1 
ATOM   2805 C  CA  . ALA B 1 63  ? -14.052 -5.219  38.699  1.00 18.52 ? 63  ALA B CA  1 
ATOM   2806 C  C   . ALA B 1 63  ? -13.009 -4.125  38.510  1.00 15.93 ? 63  ALA B C   1 
ATOM   2807 O  O   . ALA B 1 63  ? -13.288 -2.952  38.689  1.00 15.38 ? 63  ALA B O   1 
ATOM   2808 C  CB  . ALA B 1 63  ? -14.069 -5.707  40.172  1.00 20.17 ? 63  ALA B CB  1 
ATOM   2809 N  N   . HIS B 1 64  ? -11.785 -4.540  38.150  1.00 12.51 ? 64  HIS B N   1 
ATOM   2810 C  CA  . HIS B 1 64  ? -10.721 -3.578  37.944  1.00 13.63 ? 64  HIS B CA  1 
ATOM   2811 C  C   . HIS B 1 64  ? -10.275 -3.750  36.499  1.00 13.73 ? 64  HIS B C   1 
ATOM   2812 O  O   . HIS B 1 64  ? -10.375 -4.829  35.929  1.00 14.18 ? 64  HIS B O   1 
ATOM   2813 C  CB  . HIS B 1 64  ? -9.538  -3.791  38.874  1.00 14.31 ? 64  HIS B CB  1 
ATOM   2814 C  CG  . HIS B 1 64  ? -9.870  -3.879  40.335  1.00 15.07 ? 64  HIS B CG  1 
ATOM   2815 N  ND1 . HIS B 1 64  ? -10.340 -2.814  41.034  1.00 16.33 ? 64  HIS B ND1 1 
ATOM   2816 C  CD2 . HIS B 1 64  ? -9.770  -4.966  41.174  1.00 16.55 ? 64  HIS B CD2 1 
ATOM   2817 C  CE1 . HIS B 1 64  ? -10.587 -3.242  42.296  1.00 16.18 ? 64  HIS B CE1 1 
ATOM   2818 N  NE2 . HIS B 1 64  ? -10.278 -4.604  42.375  1.00 17.17 ? 64  HIS B NE2 1 
ATOM   2819 N  N   . GLN B 1 65  ? -9.671  -2.682  35.985  1.00 11.67 ? 65  GLN B N   1 
ATOM   2820 C  CA  . GLN B 1 65  ? -8.939  -2.830  34.727  1.00 11.47 ? 65  GLN B CA  1 
ATOM   2821 C  C   . GLN B 1 65  ? -7.741  -3.747  34.936  1.00 11.11 ? 65  GLN B C   1 
ATOM   2822 O  O   . GLN B 1 65  ? -7.016  -3.680  35.932  1.00 11.95 ? 65  GLN B O   1 
ATOM   2823 C  CB  . GLN B 1 65  ? -8.492  -1.486  34.138  1.00 10.41 ? 65  GLN B CB  1 
ATOM   2824 C  CG  . GLN B 1 65  ? -9.694  -0.600  33.765  1.00 10.09 ? 65  GLN B CG  1 
ATOM   2825 C  CD  . GLN B 1 65  ? -9.205  0.613   32.968  1.00 13.36 ? 65  GLN B CD  1 
ATOM   2826 O  OE1 . GLN B 1 65  ? -8.735  0.437   31.817  1.00 11.66 ? 65  GLN B OE1 1 
ATOM   2827 N  NE2 . GLN B 1 65  ? -9.323  1.807   33.541  1.00 12.60 ? 65  GLN B NE2 1 
ATOM   2828 N  N   . ALA B 1 66  ? -7.493  -4.547  33.896  1.00 11.76 ? 66  ALA B N   1 
ATOM   2829 C  CA  . ALA B 1 66  ? -6.259  -5.328  33.850  1.00 12.41 ? 66  ALA B CA  1 
ATOM   2830 C  C   . ALA B 1 66  ? -5.118  -4.366  33.560  1.00 12.05 ? 66  ALA B C   1 
ATOM   2831 O  O   . ALA B 1 66  ? -5.365  -3.258  33.117  1.00 13.76 ? 66  ALA B O   1 
ATOM   2832 C  CB  . ALA B 1 66  ? -6.338  -6.417  32.806  1.00 12.27 ? 66  ALA B CB  1 
ATOM   2833 N  N   . GLY B 1 67  ? -3.876  -4.816  33.784  1.00 11.86 ? 67  GLY B N   1 
ATOM   2834 C  CA  . GLY B 1 67  ? -2.711  -4.034  33.472  1.00 12.69 ? 67  GLY B CA  1 
ATOM   2835 C  C   . GLY B 1 67  ? -2.189  -3.243  34.671  1.00 13.15 ? 67  GLY B C   1 
ATOM   2836 O  O   . GLY B 1 67  ? -1.274  -2.433  34.533  1.00 15.53 ? 67  GLY B O   1 
ATOM   2837 N  N   . ILE B 1 68  ? -2.758  -3.491  35.878  1.00 12.49 ? 68  ILE B N   1 
ATOM   2838 C  CA  . ILE B 1 68  ? -2.318  -2.855  37.108  1.00 13.02 ? 68  ILE B CA  1 
ATOM   2839 C  C   . ILE B 1 68  ? -1.736  -3.913  38.058  1.00 16.14 ? 68  ILE B C   1 
ATOM   2840 O  O   . ILE B 1 68  ? -0.526  -3.924  38.288  1.00 15.09 ? 68  ILE B O   1 
ATOM   2841 C  CB  . ILE B 1 68  ? -3.454  -2.041  37.740  1.00 14.07 ? 68  ILE B CB  1 
ATOM   2842 C  CG1 . ILE B 1 68  ? -3.962  -1.064  36.654  1.00 17.59 ? 68  ILE B CG1 1 
ATOM   2843 C  CG2 . ILE B 1 68  ? -2.984  -1.328  39.024  1.00 17.63 ? 68  ILE B CG2 1 
ATOM   2844 C  CD1 . ILE B 1 68  ? -5.293  -0.397  36.925  1.00 19.60 ? 68  ILE B CD1 1 
ATOM   2845 N  N   . ALA B 1 69  ? -2.634  -4.778  38.520  1.00 13.60 ? 69  ALA B N   1 
ATOM   2846 C  CA  . ALA B 1 69  ? -2.314  -5.870  39.443  1.00 17.31 ? 69  ALA B CA  1 
ATOM   2847 C  C   . ALA B 1 69  ? -2.055  -7.164  38.671  1.00 17.66 ? 69  ALA B C   1 
ATOM   2848 O  O   . ALA B 1 69  ? -1.657  -8.148  39.279  1.00 24.68 ? 69  ALA B O   1 
ATOM   2849 C  CB  . ALA B 1 69  ? -3.461  -6.073  40.412  1.00 16.60 ? 69  ALA B CB  1 
ATOM   2850 N  N   . THR B 1 70  ? -2.248  -7.204  37.354  1.00 15.51 ? 70  THR B N   1 
ATOM   2851 C  CA  . THR B 1 70  ? -2.027  -8.432  36.604  1.00 16.22 ? 70  THR B CA  1 
ATOM   2852 C  C   . THR B 1 70  ? -0.531  -8.548  36.298  1.00 16.39 ? 70  THR B C   1 
ATOM   2853 O  O   . THR B 1 70  ? 0.226   -7.551  36.390  1.00 16.46 ? 70  THR B O   1 
ATOM   2854 C  CB  . THR B 1 70  ? -2.992  -8.497  35.417  1.00 19.05 ? 70  THR B CB  1 
ATOM   2855 O  OG1 . THR B 1 70  ? -2.735  -7.332  34.644  1.00 16.92 ? 70  THR B OG1 1 
ATOM   2856 C  CG2 . THR B 1 70  ? -4.487  -8.548  35.745  1.00 18.99 ? 70  THR B CG2 1 
ATOM   2857 N  N   . PRO B 1 71  ? -0.033  -9.781  35.979  1.00 15.86 ? 71  PRO B N   1 
ATOM   2858 C  CA  . PRO B 1 71  ? 1.423   -9.975  35.811  1.00 17.66 ? 71  PRO B CA  1 
ATOM   2859 C  C   . PRO B 1 71  ? 2.043   -9.012  34.790  1.00 14.78 ? 71  PRO B C   1 
ATOM   2860 O  O   . PRO B 1 71  ? 1.506   -8.734  33.711  1.00 16.40 ? 71  PRO B O   1 
ATOM   2861 C  CB  . PRO B 1 71  ? 1.572   -11.445 35.349  1.00 17.81 ? 71  PRO B CB  1 
ATOM   2862 C  CG  . PRO B 1 71  ? 0.244   -12.117 35.788  1.00 23.13 ? 71  PRO B CG  1 
ATOM   2863 C  CD  . PRO B 1 71  ? -0.813  -11.022 35.808  1.00 19.12 ? 71  PRO B CD  1 
ATOM   2864 N  N   . VAL B 1 72  ? 3.215   -8.521  35.129  1.00 14.84 ? 72  VAL B N   1 
ATOM   2865 C  CA  . VAL B 1 72  ? 3.906   -7.510  34.380  1.00 14.81 ? 72  VAL B CA  1 
ATOM   2866 C  C   . VAL B 1 72  ? 4.430   -8.122  33.069  1.00 14.00 ? 72  VAL B C   1 
ATOM   2867 O  O   . VAL B 1 72  ? 5.221   -9.096  33.081  1.00 16.96 ? 72  VAL B O   1 
ATOM   2868 C  CB  . VAL B 1 72  ? 5.019   -6.855  35.195  1.00 16.71 ? 72  VAL B CB  1 
ATOM   2869 C  CG1 . VAL B 1 72  ? 5.659   -5.758  34.378  1.00 16.96 ? 72  VAL B CG1 1 
ATOM   2870 C  CG2 . VAL B 1 72  ? 4.493   -6.268  36.521  1.00 21.89 ? 72  VAL B CG2 1 
ATOM   2871 N  N   . GLN B 1 73  ? 4.021   -7.562  31.950  1.00 12.67 ? 73  GLN B N   1 
ATOM   2872 C  CA  . GLN B 1 73  ? 4.372   -8.094  30.636  1.00 12.18 ? 73  GLN B CA  1 
ATOM   2873 C  C   . GLN B 1 73  ? 5.683   -7.460  30.202  1.00 13.79 ? 73  GLN B C   1 
ATOM   2874 O  O   . GLN B 1 73  ? 6.143   -6.450  30.735  1.00 13.04 ? 73  GLN B O   1 
ATOM   2875 C  CB  . GLN B 1 73  ? 3.290   -7.847  29.582  1.00 12.19 ? 73  GLN B CB  1 
ATOM   2876 C  CG  . GLN B 1 73  ? 1.877   -8.261  30.064  1.00 11.92 ? 73  GLN B CG  1 
ATOM   2877 C  CD  . GLN B 1 73  ? 1.045   -7.136  30.657  1.00 12.68 ? 73  GLN B CD  1 
ATOM   2878 O  OE1 . GLN B 1 73  ? 1.546   -6.374  31.509  1.00 11.06 ? 73  GLN B OE1 1 
ATOM   2879 N  NE2 . GLN B 1 73  ? -0.224  -7.057  30.242  1.00 9.60  ? 73  GLN B NE2 1 
ATOM   2880 N  N   . ASP B 1 74  ? 6.311   -8.053  29.208  1.00 12.42 ? 74  ASP B N   1 
ATOM   2881 C  CA  . ASP B 1 74  ? 7.673   -7.666  28.857  1.00 12.42 ? 74  ASP B CA  1 
ATOM   2882 C  C   . ASP B 1 74  ? 7.795   -6.332  28.159  1.00 11.31 ? 74  ASP B C   1 
ATOM   2883 O  O   . ASP B 1 74  ? 8.902   -5.746  28.196  1.00 12.65 ? 74  ASP B O   1 
ATOM   2884 C  CB  . ASP B 1 74  ? 8.276   -8.696  27.883  1.00 14.00 ? 74  ASP B CB  1 
ATOM   2885 C  CG  . ASP B 1 74  ? 8.299   -10.133 28.405  1.00 17.92 ? 74  ASP B CG  1 
ATOM   2886 O  OD1 . ASP B 1 74  ? 8.200   -10.286 29.652  1.00 20.88 ? 74  ASP B OD1 1 
ATOM   2887 O  OD2 . ASP B 1 74  ? 8.621   -11.041 27.579  1.00 18.21 ? 74  ASP B OD2 1 
ATOM   2888 N  N   . ARG B 1 75  ? 6.712   -5.823  27.535  1.00 12.21 ? 75  ARG B N   1 
ATOM   2889 C  CA  . ARG B 1 75  ? 6.834   -4.627  26.709  1.00 11.57 ? 75  ARG B CA  1 
ATOM   2890 C  C   . ARG B 1 75  ? 5.687   -3.654  26.997  1.00 12.07 ? 75  ARG B C   1 
ATOM   2891 O  O   . ARG B 1 75  ? 4.597   -4.036  27.418  1.00 13.31 ? 75  ARG B O   1 
ATOM   2892 C  CB  . ARG B 1 75  ? 6.814   -4.958  25.202  1.00 14.31 ? 75  ARG B CB  1 
ATOM   2893 C  CG  . ARG B 1 75  ? 7.806   -6.068  24.823  1.00 14.34 ? 75  ARG B CG  1 
ATOM   2894 C  CD  . ARG B 1 75  ? 9.243   -5.663  24.824  1.00 18.94 ? 75  ARG B CD  1 
ATOM   2895 N  NE  . ARG B 1 75  ? 10.049  -6.852  24.548  1.00 22.21 ? 75  ARG B NE  1 
ATOM   2896 C  CZ  . ARG B 1 75  ? 10.906  -7.415  25.395  1.00 21.68 ? 75  ARG B CZ  1 
ATOM   2897 N  NH1 . ARG B 1 75  ? 11.192  -6.870  26.567  1.00 17.65 ? 75  ARG B NH1 1 
ATOM   2898 N  NH2 . ARG B 1 75  ? 11.531  -8.506  24.986  1.00 24.14 ? 75  ARG B NH2 1 
ATOM   2899 N  N   . LEU B 1 76  ? 5.932   -2.384  26.643  1.00 11.09 ? 76  LEU B N   1 
ATOM   2900 C  CA  . LEU B 1 76  ? 5.009   -1.287  26.854  1.00 10.07 ? 76  LEU B CA  1 
ATOM   2901 C  C   . LEU B 1 76  ? 4.942   -0.401  25.628  1.00 10.65 ? 76  LEU B C   1 
ATOM   2902 O  O   . LEU B 1 76  ? 5.976   -0.024  25.060  1.00 12.77 ? 76  LEU B O   1 
ATOM   2903 C  CB  . LEU B 1 76  ? 5.451   -0.426  28.038  1.00 10.98 ? 76  LEU B CB  1 
ATOM   2904 C  CG  . LEU B 1 76  ? 4.681   0.872   28.279  1.00 13.02 ? 76  LEU B CG  1 
ATOM   2905 C  CD1 . LEU B 1 76  ? 3.330   0.642   28.858  1.00 15.25 ? 76  LEU B CD1 1 
ATOM   2906 C  CD2 . LEU B 1 76  ? 5.481   1.827   29.179  1.00 17.36 ? 76  LEU B CD2 1 
ATOM   2907 N  N   . HIS B 1 77  ? 3.726   -0.016  25.249  1.00 11.59 ? 77  HIS B N   1 
ATOM   2908 C  CA  . HIS B 1 77  ? 3.510   1.177   24.448  1.00 11.14 ? 77  HIS B CA  1 
ATOM   2909 C  C   . HIS B 1 77  ? 2.464   2.027   25.132  1.00 10.63 ? 77  HIS B C   1 
ATOM   2910 O  O   . HIS B 1 77  ? 1.299   1.601   25.323  1.00 10.56 ? 77  HIS B O   1 
ATOM   2911 C  CB  . HIS B 1 77  ? 3.025   0.805   23.039  1.00 13.07 ? 77  HIS B CB  1 
ATOM   2912 C  CG  . HIS B 1 77  ? 3.052   1.907   22.063  1.00 11.73 ? 77  HIS B CG  1 
ATOM   2913 N  ND1 . HIS B 1 77  ? 2.538   1.789   20.817  1.00 16.00 ? 77  HIS B ND1 1 
ATOM   2914 C  CD2 . HIS B 1 77  ? 3.528   3.176   22.184  1.00 19.43 ? 77  HIS B CD2 1 
ATOM   2915 C  CE1 . HIS B 1 77  ? 2.801   2.909   20.140  1.00 16.58 ? 77  HIS B CE1 1 
ATOM   2916 N  NE2 . HIS B 1 77  ? 3.449   3.774   20.952  1.00 17.96 ? 77  HIS B NE2 1 
ATOM   2917 N  N   . PHE B 1 78  ? 2.914   3.175   25.631  1.00 11.49 ? 78  PHE B N   1 
ATOM   2918 C  CA  . PHE B 1 78  ? 2.048   4.087   26.382  1.00 11.53 ? 78  PHE B CA  1 
ATOM   2919 C  C   . PHE B 1 78  ? 1.754   5.303   25.511  1.00 12.51 ? 78  PHE B C   1 
ATOM   2920 O  O   . PHE B 1 78  ? 2.663   5.870   24.918  1.00 12.29 ? 78  PHE B O   1 
ATOM   2921 C  CB  . PHE B 1 78  ? 2.760   4.505   27.660  1.00 12.87 ? 78  PHE B CB  1 
ATOM   2922 C  CG  . PHE B 1 78  ? 1.901   5.191   28.681  1.00 14.29 ? 78  PHE B CG  1 
ATOM   2923 C  CD1 . PHE B 1 78  ? 1.547   6.519   28.528  1.00 14.15 ? 78  PHE B CD1 1 
ATOM   2924 C  CD2 . PHE B 1 78  ? 1.353   4.511   29.742  1.00 14.22 ? 78  PHE B CD2 1 
ATOM   2925 C  CE1 . PHE B 1 78  ? 0.801   7.176   29.505  1.00 15.14 ? 78  PHE B CE1 1 
ATOM   2926 C  CE2 . PHE B 1 78  ? 0.539   5.143   30.663  1.00 14.07 ? 78  PHE B CE2 1 
ATOM   2927 C  CZ  . PHE B 1 78  ? 0.295   6.503   30.559  1.00 14.15 ? 78  PHE B CZ  1 
ATOM   2928 N  N   . ALA B 1 79  ? 0.470   5.630   25.324  1.00 11.85 ? 79  ALA B N   1 
ATOM   2929 C  CA  . ALA B 1 79  ? 0.160   6.802   24.534  1.00 12.59 ? 79  ALA B CA  1 
ATOM   2930 C  C   . ALA B 1 79  ? -0.773  7.719   25.309  1.00 12.19 ? 79  ALA B C   1 
ATOM   2931 O  O   . ALA B 1 79  ? -1.772  7.284   25.924  1.00 11.84 ? 79  ALA B O   1 
ATOM   2932 C  CB  . ALA B 1 79  ? -0.415  6.438   23.205  1.00 14.11 ? 79  ALA B CB  1 
ATOM   2933 N  N   . ALA B 1 80  ? -0.467  9.029   25.221  1.00 10.28 ? 80  ALA B N   1 
ATOM   2934 C  CA  . ALA B 1 80  ? -1.343  10.069  25.739  1.00 10.39 ? 80  ALA B CA  1 
ATOM   2935 C  C   . ALA B 1 80  ? -2.074  10.659  24.547  1.00 11.17 ? 80  ALA B C   1 
ATOM   2936 O  O   . ALA B 1 80  ? -1.439  10.901  23.500  1.00 12.87 ? 80  ALA B O   1 
ATOM   2937 C  CB  . ALA B 1 80  ? -0.623  11.166  26.517  1.00 10.36 ? 80  ALA B CB  1 
ATOM   2938 N  N   . PHE B 1 81  ? -3.366  10.922  24.721  1.00 10.43 ? 81  PHE B N   1 
ATOM   2939 C  CA  . PHE B 1 81  ? -4.168  11.483  23.654  1.00 11.79 ? 81  PHE B CA  1 
ATOM   2940 C  C   . PHE B 1 81  ? -4.802  12.776  24.139  1.00 14.04 ? 81  PHE B C   1 
ATOM   2941 O  O   . PHE B 1 81  ? -5.130  12.920  25.329  1.00 12.94 ? 81  PHE B O   1 
ATOM   2942 C  CB  . PHE B 1 81  ? -5.321  10.600  23.235  1.00 12.36 ? 81  PHE B CB  1 
ATOM   2943 C  CG  . PHE B 1 81  ? -4.948  9.249   22.674  1.00 13.76 ? 81  PHE B CG  1 
ATOM   2944 C  CD1 . PHE B 1 81  ? -4.609  8.198   23.511  1.00 14.81 ? 81  PHE B CD1 1 
ATOM   2945 C  CD2 . PHE B 1 81  ? -5.012  9.053   21.306  1.00 15.63 ? 81  PHE B CD2 1 
ATOM   2946 C  CE1 . PHE B 1 81  ? -4.272  6.977   22.950  1.00 17.56 ? 81  PHE B CE1 1 
ATOM   2947 C  CE2 . PHE B 1 81  ? -4.646  7.825   20.770  1.00 18.21 ? 81  PHE B CE2 1 
ATOM   2948 C  CZ  . PHE B 1 81  ? -4.292  6.801   21.610  1.00 15.14 ? 81  PHE B CZ  1 
ATOM   2949 N  N   . ASP B 1 82  ? -4.930  13.728  23.207  1.00 14.89 ? 82  ASP B N   1 
ATOM   2950 C  CA  . ASP B 1 82  ? -5.790  14.886  23.459  1.00 15.11 ? 82  ASP B CA  1 
ATOM   2951 C  C   . ASP B 1 82  ? -7.095  14.775  22.678  1.00 13.78 ? 82  ASP B C   1 
ATOM   2952 O  O   . ASP B 1 82  ? -7.153  14.177  21.597  1.00 14.85 ? 82  ASP B O   1 
ATOM   2953 C  CB  . ASP B 1 82  ? -5.058  16.168  23.075  1.00 14.03 ? 82  ASP B CB  1 
ATOM   2954 C  CG  . ASP B 1 82  ? -3.978  16.542  24.077  1.00 15.93 ? 82  ASP B CG  1 
ATOM   2955 O  OD1 . ASP B 1 82  ? -4.038  16.124  25.265  1.00 17.24 ? 82  ASP B OD1 1 
ATOM   2956 O  OD2 . ASP B 1 82  ? -3.137  17.254  23.650  1.00 16.12 ? 82  ASP B OD2 1 
ATOM   2957 N  N   . VAL B 1 83  ? -8.173  15.294  23.265  1.00 16.81 ? 83  VAL B N   1 
ATOM   2958 C  CA  . VAL B 1 83  ? -9.498  15.207  22.672  1.00 15.43 ? 83  VAL B CA  1 
ATOM   2959 C  C   . VAL B 1 83  ? -9.706  16.478  21.848  1.00 19.63 ? 83  VAL B C   1 
ATOM   2960 O  O   . VAL B 1 83  ? -9.415  17.594  22.316  1.00 19.87 ? 83  VAL B O   1 
ATOM   2961 C  CB  . VAL B 1 83  ? -10.535 15.055  23.809  1.00 17.89 ? 83  VAL B CB  1 
ATOM   2962 C  CG1 . VAL B 1 83  ? -11.943 15.136  23.305  1.00 20.32 ? 83  VAL B CG1 1 
ATOM   2963 C  CG2 . VAL B 1 83  ? -10.306 13.774  24.605  1.00 19.09 ? 83  VAL B CG2 1 
ATOM   2964 N  N   . THR B 1 84  ? -10.183 16.316  20.607  1.00 18.18 ? 84  THR B N   1 
ATOM   2965 C  CA  . THR B 1 84  ? -10.437 17.415  19.677  1.00 19.01 ? 84  THR B CA  1 
ATOM   2966 C  C   . THR B 1 84  ? -11.936 17.726  19.528  1.00 24.66 ? 84  THR B C   1 
ATOM   2967 O  O   . THR B 1 84  ? -12.248 18.735  18.930  1.00 30.56 ? 84  THR B O   1 
ATOM   2968 C  CB  . THR B 1 84  ? -9.701  17.210  18.347  1.00 19.24 ? 84  THR B CB  1 
ATOM   2969 O  OG1 . THR B 1 84  ? -10.311 16.053  17.761  1.00 22.29 ? 84  THR B OG1 1 
ATOM   2970 C  CG2 . THR B 1 84  ? -8.191  17.070  18.569  1.00 21.71 ? 84  THR B CG2 1 
ATOM   2971 N  N   . THR B 1 85  ? -12.848 16.885  20.026  1.00 18.43 ? 85  THR B N   1 
ATOM   2972 C  CA  . THR B 1 85  ? -14.264 17.185  19.979  1.00 18.78 ? 85  THR B CA  1 
ATOM   2973 C  C   . THR B 1 85  ? -14.764 17.843  21.283  1.00 19.77 ? 85  THR B C   1 
ATOM   2974 O  O   . THR B 1 85  ? -14.268 17.591  22.374  1.00 21.37 ? 85  THR B O   1 
ATOM   2975 C  CB  . THR B 1 85  ? -15.021 15.896  19.619  1.00 21.01 ? 85  THR B CB  1 
ATOM   2976 O  OG1 . THR B 1 85  ? -16.392 16.246  19.562  1.00 24.59 ? 85  THR B OG1 1 
ATOM   2977 C  CG2 . THR B 1 85  ? -14.820 14.814  20.645  1.00 21.99 ? 85  THR B CG2 1 
ATOM   2978 N  N   . GLU B 1 86  ? -15.797 18.696  21.154  1.00 19.06 ? 86  GLU B N   1 
ATOM   2979 C  CA  . GLU B 1 86  ? -16.509 19.265  22.293  1.00 21.86 ? 86  GLU B CA  1 
ATOM   2980 C  C   . GLU B 1 86  ? -17.828 18.553  22.575  1.00 21.27 ? 86  GLU B C   1 
ATOM   2981 O  O   . GLU B 1 86  ? -18.503 18.869  23.559  1.00 22.96 ? 86  GLU B O   1 
ATOM   2982 C  CB  . GLU B 1 86  ? -16.953 20.716  21.989  1.00 24.44 ? 86  GLU B CB  1 
ATOM   2983 C  CG  . GLU B 1 86  ? -15.825 21.619  21.625  1.00 26.82 ? 86  GLU B CG  1 
ATOM   2984 C  CD  . GLU B 1 86  ? -16.203 23.079  21.304  1.00 26.99 ? 86  GLU B CD  1 
ATOM   2985 O  OE1 . GLU B 1 86  ? -17.420 23.462  21.289  1.00 25.91 ? 86  GLU B OE1 1 
ATOM   2986 O  OE2 . GLU B 1 86  ? -15.269 23.830  21.117  1.00 30.96 ? 86  GLU B OE2 1 
ATOM   2987 N  N   . ASP B 1 87  ? -18.180 17.584  21.739  1.00 19.09 ? 87  ASP B N   1 
ATOM   2988 C  CA  . ASP B 1 87  ? -19.469 16.917  21.793  1.00 20.12 ? 87  ASP B CA  1 
ATOM   2989 C  C   . ASP B 1 87  ? -19.342 15.674  22.674  1.00 21.64 ? 87  ASP B C   1 
ATOM   2990 O  O   . ASP B 1 87  ? -18.653 14.736  22.267  1.00 20.32 ? 87  ASP B O   1 
ATOM   2991 C  CB  . ASP B 1 87  ? -19.845 16.515  20.372  1.00 21.72 ? 87  ASP B CB  1 
ATOM   2992 C  CG  . ASP B 1 87  ? -21.175 15.803  20.187  1.00 25.04 ? 87  ASP B CG  1 
ATOM   2993 O  OD1 . ASP B 1 87  ? -21.800 15.452  21.185  1.00 36.09 ? 87  ASP B OD1 1 
ATOM   2994 O  OD2 . ASP B 1 87  ? -21.558 15.623  19.056  1.00 35.13 ? 87  ASP B OD2 1 
ATOM   2995 N  N   . ARG B 1 88  ? -20.035 15.691  23.808  1.00 22.06 ? 88  ARG B N   1 
ATOM   2996 C  CA  . ARG B 1 88  ? -20.010 14.636  24.798  1.00 22.51 ? 88  ARG B CA  1 
ATOM   2997 C  C   . ARG B 1 88  ? -20.506 13.330  24.191  1.00 21.22 ? 88  ARG B C   1 
ATOM   2998 O  O   . ARG B 1 88  ? -19.927 12.275  24.434  1.00 20.32 ? 88  ARG B O   1 
ATOM   2999 C  CB  . ARG B 1 88  ? -20.818 15.027  26.036  1.00 25.56 ? 88  ARG B CB  1 
ATOM   3000 C  CG  . ARG B 1 88  ? -20.929 13.969  27.137  1.00 27.94 ? 88  ARG B CG  1 
ATOM   3001 C  CD  . ARG B 1 88  ? -21.699 14.563  28.290  1.00 30.18 ? 88  ARG B CD  1 
ATOM   3002 N  NE  . ARG B 1 88  ? -22.135 13.615  29.268  1.00 36.24 ? 88  ARG B NE  1 
ATOM   3003 C  CZ  . ARG B 1 88  ? -21.771 13.650  30.542  1.00 43.00 ? 88  ARG B CZ  1 
ATOM   3004 N  NH1 . ARG B 1 88  ? -21.173 14.729  31.034  1.00 37.97 ? 88  ARG B NH1 1 
ATOM   3005 N  NH2 . ARG B 1 88  ? -22.006 12.590  31.313  1.00 40.80 ? 88  ARG B NH2 1 
ATOM   3006 N  N   . ALA B 1 89  ? -21.553 13.426  23.355  1.00 20.37 ? 89  ALA B N   1 
ATOM   3007 C  CA  . ALA B 1 89  ? -22.149 12.268  22.729  1.00 20.53 ? 89  ALA B CA  1 
ATOM   3008 C  C   . ALA B 1 89  ? -21.148 11.589  21.799  1.00 19.18 ? 89  ALA B C   1 
ATOM   3009 O  O   . ALA B 1 89  ? -21.051 10.358  21.750  1.00 17.69 ? 89  ALA B O   1 
ATOM   3010 C  CB  . ALA B 1 89  ? -23.443 12.645  21.999  1.00 23.33 ? 89  ALA B CB  1 
ATOM   3011 N  N   . ALA B 1 90  ? -20.401 12.384  21.053  1.00 16.48 ? 90  ALA B N   1 
ATOM   3012 C  CA  . ALA B 1 90  ? -19.422 11.827  20.119  1.00 19.19 ? 90  ALA B CA  1 
ATOM   3013 C  C   . ALA B 1 90  ? -18.273 11.177  20.894  1.00 17.76 ? 90  ALA B C   1 
ATOM   3014 O  O   . ALA B 1 90  ? -17.801 10.111  20.493  1.00 17.03 ? 90  ALA B O   1 
ATOM   3015 C  CB  . ALA B 1 90  ? -18.940 12.892  19.166  1.00 24.05 ? 90  ALA B CB  1 
ATOM   3016 N  N   . PHE B 1 91  ? -17.941 11.715  22.073  1.00 17.99 ? 91  PHE B N   1 
ATOM   3017 C  CA  . PHE B 1 91  ? -16.858 11.136  22.867  1.00 16.46 ? 91  PHE B CA  1 
ATOM   3018 C  C   . PHE B 1 91  ? -17.317 9.825   23.508  1.00 17.88 ? 91  PHE B C   1 
ATOM   3019 O  O   . PHE B 1 91  ? -16.564 8.841   23.535  1.00 15.86 ? 91  PHE B O   1 
ATOM   3020 C  CB  . PHE B 1 91  ? -16.409 12.150  23.910  1.00 18.29 ? 91  PHE B CB  1 
ATOM   3021 C  CG  . PHE B 1 91  ? -15.191 11.649  24.634  1.00 18.16 ? 91  PHE B CG  1 
ATOM   3022 C  CD1 . PHE B 1 91  ? -13.986 11.586  23.969  1.00 20.89 ? 91  PHE B CD1 1 
ATOM   3023 C  CD2 . PHE B 1 91  ? -15.265 11.285  25.959  1.00 19.74 ? 91  PHE B CD2 1 
ATOM   3024 C  CE1 . PHE B 1 91  ? -12.884 11.080  24.626  1.00 20.22 ? 91  PHE B CE1 1 
ATOM   3025 C  CE2 . PHE B 1 91  ? -14.146 10.817  26.634  1.00 20.99 ? 91  PHE B CE2 1 
ATOM   3026 C  CZ  . PHE B 1 91  ? -12.973 10.672  25.935  1.00 20.39 ? 91  PHE B CZ  1 
ATOM   3027 N  N   . VAL B 1 92  ? -18.580 9.785   24.011  1.00 15.75 ? 92  VAL B N   1 
ATOM   3028 C  CA  . VAL B 1 92  ? -19.134 8.555   24.562  1.00 18.44 ? 92  VAL B CA  1 
ATOM   3029 C  C   . VAL B 1 92  ? -19.132 7.438   23.516  1.00 16.21 ? 92  VAL B C   1 
ATOM   3030 O  O   . VAL B 1 92  ? -18.742 6.284   23.791  1.00 15.22 ? 92  VAL B O   1 
ATOM   3031 C  CB  . VAL B 1 92  ? -20.516 8.786   25.213  1.00 17.47 ? 92  VAL B CB  1 
ATOM   3032 C  CG1 . VAL B 1 92  ? -21.188 7.474   25.524  1.00 21.38 ? 92  VAL B CG1 1 
ATOM   3033 C  CG2 . VAL B 1 92  ? -20.313 9.565   26.482  1.00 18.17 ? 92  VAL B CG2 1 
ATOM   3034 N  N   . ALA B 1 93  ? -19.499 7.815   22.280  1.00 14.81 ? 93  ALA B N   1 
ATOM   3035 C  CA  . ALA B 1 93  ? -19.579 6.877   21.186  1.00 16.99 ? 93  ALA B CA  1 
ATOM   3036 C  C   . ALA B 1 93  ? -18.197 6.293   20.899  1.00 15.25 ? 93  ALA B C   1 
ATOM   3037 O  O   . ALA B 1 93  ? -18.052 5.110   20.617  1.00 17.58 ? 93  ALA B O   1 
ATOM   3038 C  CB  . ALA B 1 93  ? -20.097 7.593   19.929  1.00 17.02 ? 93  ALA B CB  1 
ATOM   3039 N  N   . LEU B 1 94  ? -17.179 7.143   21.000  1.00 15.13 ? 94  LEU B N   1 
ATOM   3040 C  CA  . LEU B 1 94  ? -15.803 6.722   20.820  1.00 14.05 ? 94  LEU B CA  1 
ATOM   3041 C  C   . LEU B 1 94  ? -15.361 5.746   21.922  1.00 13.81 ? 94  LEU B C   1 
ATOM   3042 O  O   . LEU B 1 94  ? -14.760 4.711   21.627  1.00 15.94 ? 94  LEU B O   1 
ATOM   3043 C  CB  . LEU B 1 94  ? -14.855 7.908   20.770  1.00 16.73 ? 94  LEU B CB  1 
ATOM   3044 C  CG  . LEU B 1 94  ? -13.367 7.543   20.736  1.00 19.61 ? 94  LEU B CG  1 
ATOM   3045 C  CD1 . LEU B 1 94  ? -12.979 6.918   19.408  1.00 21.33 ? 94  LEU B CD1 1 
ATOM   3046 C  CD2 . LEU B 1 94  ? -12.508 8.778   21.042  1.00 23.42 ? 94  LEU B CD2 1 
ATOM   3047 N  N   . LEU B 1 95  ? -15.687 6.046   23.191  1.00 13.87 ? 95  LEU B N   1 
ATOM   3048 C  CA  . LEU B 1 95  ? -15.330 5.117   24.279  1.00 13.21 ? 95  LEU B CA  1 
ATOM   3049 C  C   . LEU B 1 95  ? -15.952 3.761   24.046  1.00 13.89 ? 95  LEU B C   1 
ATOM   3050 O  O   . LEU B 1 95  ? -15.317 2.760   24.321  1.00 13.74 ? 95  LEU B O   1 
ATOM   3051 C  CB  . LEU B 1 95  ? -15.781 5.651   25.632  1.00 14.17 ? 95  LEU B CB  1 
ATOM   3052 C  CG  . LEU B 1 95  ? -15.018 6.903   26.076  1.00 14.45 ? 95  LEU B CG  1 
ATOM   3053 C  CD1 . LEU B 1 95  ? -15.640 7.455   27.330  1.00 17.00 ? 95  LEU B CD1 1 
ATOM   3054 C  CD2 . LEU B 1 95  ? -13.607 6.565   26.341  1.00 16.78 ? 95  LEU B CD2 1 
ATOM   3055 N  N   . LYS B 1 96  ? -17.204 3.725   23.551  1.00 15.59 ? 96  LYS B N   1 
ATOM   3056 C  CA  . LYS B 1 96  ? -17.833 2.434   23.294  1.00 15.36 ? 96  LYS B CA  1 
ATOM   3057 C  C   . LYS B 1 96  ? -17.134 1.714   22.165  1.00 13.91 ? 96  LYS B C   1 
ATOM   3058 O  O   . LYS B 1 96  ? -16.924 0.525   22.250  1.00 14.23 ? 96  LYS B O   1 
ATOM   3059 C  CB  . LYS B 1 96  ? -19.321 2.590   22.967  1.00 18.49 ? 96  LYS B CB  1 
ATOM   3060 C  CG  . LYS B 1 96  ? -20.072 3.130   24.157  1.00 20.14 ? 96  LYS B CG  1 
ATOM   3061 C  CD  . LYS B 1 96  ? -21.508 3.421   23.836  1.00 19.35 ? 96  LYS B CD  1 
ATOM   3062 C  CE  . LYS B 1 96  ? -22.294 3.729   25.075  1.00 24.49 ? 96  LYS B CE  1 
ATOM   3063 N  NZ  . LYS B 1 96  ? -23.708 3.880   24.737  1.00 27.36 ? 96  LYS B NZ  1 
ATOM   3064 N  N   . GLU B 1 97  ? -16.751 2.408   21.103  1.00 13.32 ? 97  GLU B N   1 
ATOM   3065 C  CA  . GLU B 1 97  ? -16.104 1.747   19.952  1.00 15.69 ? 97  GLU B CA  1 
ATOM   3066 C  C   . GLU B 1 97  ? -14.734 1.257   20.379  1.00 14.52 ? 97  GLU B C   1 
ATOM   3067 O  O   . GLU B 1 97  ? -14.278 0.181   19.940  1.00 13.12 ? 97  GLU B O   1 
ATOM   3068 C  CB  . GLU B 1 97  ? -15.882 2.691   18.766  1.00 18.64 ? 97  GLU B CB  1 
ATOM   3069 C  CG  . GLU B 1 97  ? -17.061 3.009   17.910  1.00 24.34 ? 97  GLU B CG  1 
ATOM   3070 C  CD  . GLU B 1 97  ? -16.502 3.743   16.670  1.00 32.19 ? 97  GLU B CD  1 
ATOM   3071 O  OE1 . GLU B 1 97  ? -15.890 3.076   15.766  1.00 35.51 ? 97  GLU B OE1 1 
ATOM   3072 O  OE2 . GLU B 1 97  ? -16.470 4.977   16.724  1.00 42.60 ? 97  GLU B OE2 1 
ATOM   3073 N  N   . TRP B 1 98  ? -14.026 2.069   21.189  1.00 12.77 ? 98  TRP B N   1 
ATOM   3074 C  CA  . TRP B 1 98  ? -12.730 1.674   21.719  1.00 14.08 ? 98  TRP B CA  1 
ATOM   3075 C  C   . TRP B 1 98  ? -12.839 0.423   22.590  1.00 13.16 ? 98  TRP B C   1 
ATOM   3076 O  O   . TRP B 1 98  ? -11.950 -0.419  22.552  1.00 13.72 ? 98  TRP B O   1 
ATOM   3077 C  CB  . TRP B 1 98  ? -12.068 2.794   22.502  1.00 12.63 ? 98  TRP B CB  1 
ATOM   3078 C  CG  . TRP B 1 98  ? -11.257 3.718   21.666  1.00 15.14 ? 98  TRP B CG  1 
ATOM   3079 C  CD1 . TRP B 1 98  ? -11.063 3.711   20.299  1.00 13.22 ? 98  TRP B CD1 1 
ATOM   3080 C  CD2 . TRP B 1 98  ? -10.314 4.656   22.197  1.00 17.28 ? 98  TRP B CD2 1 
ATOM   3081 N  NE1 . TRP B 1 98  ? -10.146 4.648   19.969  1.00 15.28 ? 98  TRP B NE1 1 
ATOM   3082 C  CE2 . TRP B 1 98  ? -9.667  5.257   21.102  1.00 13.88 ? 98  TRP B CE2 1 
ATOM   3083 C  CE3 . TRP B 1 98  ? -10.009 5.094   23.496  1.00 19.27 ? 98  TRP B CE3 1 
ATOM   3084 C  CZ2 . TRP B 1 98  ? -8.669  6.228   21.276  1.00 18.02 ? 98  TRP B CZ2 1 
ATOM   3085 C  CZ3 . TRP B 1 98  ? -9.038  6.056   23.652  1.00 23.08 ? 98  TRP B CZ3 1 
ATOM   3086 C  CH2 . TRP B 1 98  ? -8.393  6.625   22.548  1.00 19.52 ? 98  TRP B CH2 1 
ATOM   3087 N  N   . THR B 1 99  ? -13.874 0.375   23.432  1.00 12.62 ? 99  THR B N   1 
ATOM   3088 C  CA  . THR B 1 99  ? -14.072 -0.772  24.272  1.00 12.54 ? 99  THR B CA  1 
ATOM   3089 C  C   . THR B 1 99  ? -14.320 -2.035  23.457  1.00 12.72 ? 99  THR B C   1 
ATOM   3090 O  O   . THR B 1 99  ? -13.751 -3.103  23.727  1.00 15.20 ? 99  THR B O   1 
ATOM   3091 C  CB  . THR B 1 99  ? -15.213 -0.607  25.267  1.00 14.59 ? 99  THR B CB  1 
ATOM   3092 O  OG1 . THR B 1 99  ? -15.054 0.608   26.018  1.00 15.69 ? 99  THR B OG1 1 
ATOM   3093 C  CG2 . THR B 1 99  ? -15.184 -1.788  26.214  1.00 15.04 ? 99  THR B CG2 1 
ATOM   3094 N  N   . ALA B 1 100 ? -15.111 -1.911  22.390  1.00 12.41 ? 100 ALA B N   1 
ATOM   3095 C  CA  . ALA B 1 100 ? -15.327 -3.051  21.489  1.00 15.15 ? 100 ALA B CA  1 
ATOM   3096 C  C   . ALA B 1 100 ? -14.019 -3.490  20.818  1.00 13.72 ? 100 ALA B C   1 
ATOM   3097 O  O   . ALA B 1 100 ? -13.715 -4.664  20.760  1.00 13.05 ? 100 ALA B O   1 
ATOM   3098 C  CB  . ALA B 1 100 ? -16.415 -2.747  20.480  1.00 15.97 ? 100 ALA B CB  1 
ATOM   3099 N  N   . ALA B 1 101 ? -13.212 -2.535  20.377  1.00 13.34 ? 101 ALA B N   1 
ATOM   3100 C  CA  . ALA B 1 101 ? -11.911 -2.840  19.790  1.00 12.40 ? 101 ALA B CA  1 
ATOM   3101 C  C   . ALA B 1 101 ? -10.987 -3.504  20.813  1.00 11.23 ? 101 ALA B C   1 
ATOM   3102 O  O   . ALA B 1 101 ? -10.313 -4.495  20.475  1.00 13.08 ? 101 ALA B O   1 
ATOM   3103 C  CB  . ALA B 1 101 ? -11.292 -1.583  19.296  1.00 14.32 ? 101 ALA B CB  1 
ATOM   3104 N  N   . ALA B 1 102 ? -11.015 -3.039  22.087  1.00 11.72 ? 102 ALA B N   1 
ATOM   3105 C  CA  . ALA B 1 102 ? -10.100 -3.568  23.106  1.00 11.49 ? 102 ALA B CA  1 
ATOM   3106 C  C   . ALA B 1 102 ? -10.445 -5.036  23.330  1.00 12.68 ? 102 ALA B C   1 
ATOM   3107 O  O   . ALA B 1 102 ? -9.579  -5.876  23.562  1.00 14.61 ? 102 ALA B O   1 
ATOM   3108 C  CB  . ALA B 1 102 ? -10.237 -2.752  24.399  1.00 11.67 ? 102 ALA B CB  1 
ATOM   3109 N  N   . ARG B 1 103 ? -11.736 -5.356  23.404  1.00 12.72 ? 103 ARG B N   1 
ATOM   3110 C  CA  . ARG B 1 103 ? -12.159 -6.743  23.606  1.00 16.01 ? 103 ARG B CA  1 
ATOM   3111 C  C   . ARG B 1 103 ? -11.613 -7.673  22.533  1.00 15.79 ? 103 ARG B C   1 
ATOM   3112 O  O   . ARG B 1 103 ? -11.166 -8.776  22.866  1.00 17.27 ? 103 ARG B O   1 
ATOM   3113 C  CB  . ARG B 1 103 ? -13.664 -6.941  23.539  1.00 19.48 ? 103 ARG B CB  1 
ATOM   3114 C  CG  . ARG B 1 103 ? -14.370 -6.379  24.740  1.00 20.24 ? 103 ARG B CG  1 
ATOM   3115 C  CD  . ARG B 1 103 ? -15.819 -6.863  24.661  1.00 22.87 ? 103 ARG B CD  1 
ATOM   3116 N  NE  . ARG B 1 103 ? -16.403 -6.223  25.783  1.00 20.20 ? 103 ARG B NE  1 
ATOM   3117 C  CZ  . ARG B 1 103 ? -17.078 -5.072  25.808  1.00 22.02 ? 103 ARG B CZ  1 
ATOM   3118 N  NH1 . ARG B 1 103 ? -17.440 -4.427  24.706  1.00 19.35 ? 103 ARG B NH1 1 
ATOM   3119 N  NH2 . ARG B 1 103 ? -17.460 -4.607  26.996  1.00 21.58 ? 103 ARG B NH2 1 
ATOM   3120 N  N   . ARG B 1 104 ? -11.585 -7.201  21.289  1.00 15.81 ? 104 ARG B N   1 
ATOM   3121 C  CA  . ARG B 1 104 ? -11.005 -7.971  20.188  1.00 15.99 ? 104 ARG B CA  1 
ATOM   3122 C  C   . ARG B 1 104 ? -9.475  -8.077  20.322  1.00 14.47 ? 104 ARG B C   1 
ATOM   3123 O  O   . ARG B 1 104 ? -8.913  -9.178  20.288  1.00 15.48 ? 104 ARG B O   1 
ATOM   3124 C  CB  . ARG B 1 104 ? -11.354 -7.313  18.840  1.00 17.52 ? 104 ARG B CB  1 
ATOM   3125 C  CG  . ARG B 1 104 ? -12.817 -7.413  18.382  1.00 23.38 ? 104 ARG B CG  1 
ATOM   3126 C  CD  . ARG B 1 104 ? -13.079 -8.859  18.026  1.00 31.32 ? 104 ARG B CD  1 
ATOM   3127 N  NE  . ARG B 1 104 ? -14.357 -8.894  17.383  1.00 39.12 ? 104 ARG B NE  1 
ATOM   3128 C  CZ  . ARG B 1 104 ? -14.622 -8.226  16.261  1.00 46.60 ? 104 ARG B CZ  1 
ATOM   3129 N  NH1 . ARG B 1 104 ? -13.642 -7.791  15.483  1.00 42.71 ? 104 ARG B NH1 1 
ATOM   3130 N  NH2 . ARG B 1 104 ? -15.880 -8.004  15.916  1.00 37.68 ? 104 ARG B NH2 1 
ATOM   3131 N  N   . LEU B 1 105 ? -8.823  -6.901  20.559  1.00 13.05 ? 105 LEU B N   1 
ATOM   3132 C  CA  . LEU B 1 105 ? -7.396  -6.842  20.589  1.00 11.23 ? 105 LEU B CA  1 
ATOM   3133 C  C   . LEU B 1 105 ? -6.826  -7.761  21.673  1.00 12.45 ? 105 LEU B C   1 
ATOM   3134 O  O   . LEU B 1 105 ? -5.830  -8.413  21.427  1.00 12.39 ? 105 LEU B O   1 
ATOM   3135 C  CB  . LEU B 1 105 ? -6.948  -5.387  20.781  1.00 11.11 ? 105 LEU B CB  1 
ATOM   3136 C  CG  . LEU B 1 105 ? -7.245  -4.460  19.598  1.00 12.92 ? 105 LEU B CG  1 
ATOM   3137 C  CD1 . LEU B 1 105 ? -7.147  -2.996  20.003  1.00 13.27 ? 105 LEU B CD1 1 
ATOM   3138 C  CD2 . LEU B 1 105 ? -6.260  -4.682  18.442  1.00 15.83 ? 105 LEU B CD2 1 
ATOM   3139 N  N   . THR B 1 106 ? -7.358  -7.728  22.879  1.00 12.36 ? 106 THR B N   1 
ATOM   3140 C  CA  . THR B 1 106 ? -6.809  -8.472  24.005  1.00 13.54 ? 106 THR B CA  1 
ATOM   3141 C  C   . THR B 1 106 ? -7.074  -9.977  23.871  1.00 15.61 ? 106 THR B C   1 
ATOM   3142 O  O   . THR B 1 106 ? -6.443  -10.742 24.570  1.00 17.96 ? 106 THR B O   1 
ATOM   3143 C  CB  . THR B 1 106 ? -7.375  -7.928  25.333  1.00 13.55 ? 106 THR B CB  1 
ATOM   3144 O  OG1 . THR B 1 106 ? -8.823  -8.032  25.286  1.00 13.63 ? 106 THR B OG1 1 
ATOM   3145 C  CG2 . THR B 1 106 ? -6.937  -6.499  25.559  1.00 16.56 ? 106 THR B CG2 1 
ATOM   3146 N  N   . ALA B 1 107 ? -7.950  -10.411 22.936  1.00 14.27 ? 107 ALA B N   1 
ATOM   3147 C  CA  . ALA B 1 107 ? -8.134  -11.834 22.635  1.00 15.14 ? 107 ALA B CA  1 
ATOM   3148 C  C   . ALA B 1 107 ? -7.360  -12.255 21.392  1.00 18.65 ? 107 ALA B C   1 
ATOM   3149 O  O   . ALA B 1 107 ? -7.389  -13.430 21.036  1.00 18.92 ? 107 ALA B O   1 
ATOM   3150 C  CB  . ALA B 1 107 ? -9.612  -12.109 22.493  1.00 17.92 ? 107 ALA B CB  1 
ATOM   3151 N  N   . GLY B 1 108 ? -6.542  -11.366 20.813  1.00 15.22 ? 108 GLY B N   1 
ATOM   3152 C  CA  . GLY B 1 108 ? -5.705  -11.622 19.647  1.00 14.34 ? 108 GLY B CA  1 
ATOM   3153 C  C   . GLY B 1 108 ? -6.512  -11.626 18.373  1.00 16.67 ? 108 GLY B C   1 
ATOM   3154 O  O   . GLY B 1 108 ? -6.061  -12.154 17.380  1.00 20.95 ? 108 GLY B O   1 
ATOM   3155 N  N   . HIS B 1 109 ? -7.689  -11.009 18.376  1.00 16.64 ? 109 HIS B N   1 
ATOM   3156 C  CA  . HIS B 1 109 ? -8.475  -10.848 17.153  1.00 18.31 ? 109 HIS B CA  1 
ATOM   3157 C  C   . HIS B 1 109 ? -8.321  -9.450  16.588  1.00 17.82 ? 109 HIS B C   1 
ATOM   3158 O  O   . HIS B 1 109 ? -8.091  -8.477  17.289  1.00 15.82 ? 109 HIS B O   1 
ATOM   3159 C  CB  . HIS B 1 109 ? -9.975  -11.104 17.402  1.00 23.13 ? 109 HIS B CB  1 
ATOM   3160 C  CG  . HIS B 1 109 ? -10.238 -12.412 18.081  1.00 32.17 ? 109 HIS B CG  1 
ATOM   3161 N  ND1 . HIS B 1 109 ? -9.709  -13.619 17.659  1.00 40.14 ? 109 HIS B ND1 1 
ATOM   3162 C  CD2 . HIS B 1 109 ? -10.978 -12.657 19.190  1.00 34.14 ? 109 HIS B CD2 1 
ATOM   3163 C  CE1 . HIS B 1 109 ? -10.094 -14.573 18.503  1.00 35.51 ? 109 HIS B CE1 1 
ATOM   3164 N  NE2 . HIS B 1 109 ? -10.871 -13.990 19.477  1.00 35.12 ? 109 HIS B NE2 1 
ATOM   3165 N  N   . ALA B 1 110 ? -8.528  -9.350  15.284  1.00 16.35 ? 110 ALA B N   1 
ATOM   3166 C  CA  . ALA B 1 110 ? -8.522  -8.087  14.565  1.00 17.88 ? 110 ALA B CA  1 
ATOM   3167 C  C   . ALA B 1 110 ? -9.766  -7.275  14.932  1.00 18.66 ? 110 ALA B C   1 
ATOM   3168 O  O   . ALA B 1 110 ? -10.796 -7.839  15.307  1.00 16.01 ? 110 ALA B O   1 
ATOM   3169 C  CB  . ALA B 1 110 ? -8.460  -8.373  13.054  1.00 19.62 ? 110 ALA B CB  1 
ATOM   3170 N  N   . VAL B 1 111 ? -9.619  -5.956  14.855  1.00 16.67 ? 111 VAL B N   1 
ATOM   3171 C  CA  . VAL B 1 111 ? -10.714 -5.024  15.091  1.00 16.07 ? 111 VAL B CA  1 
ATOM   3172 C  C   . VAL B 1 111 ? -11.752 -5.073  13.959  1.00 17.84 ? 111 VAL B C   1 
ATOM   3173 O  O   . VAL B 1 111 ? -11.435 -5.276  12.776  1.00 16.52 ? 111 VAL B O   1 
ATOM   3174 C  CB  . VAL B 1 111 ? -10.254 -3.586  15.426  1.00 21.67 ? 111 VAL B CB  1 
ATOM   3175 C  CG1 . VAL B 1 111 ? -9.258  -3.598  16.563  1.00 21.70 ? 111 VAL B CG1 1 
ATOM   3176 C  CG2 . VAL B 1 111 ? -9.666  -2.845  14.295  1.00 25.31 ? 111 VAL B CG2 1 
ATOM   3177 N  N   . GLY B 1 112 ? -13.032 -4.828  14.350  1.00 17.12 ? 112 GLY B N   1 
ATOM   3178 C  CA  . GLY B 1 112 ? -14.080 -4.597  13.364  1.00 22.22 ? 112 GLY B CA  1 
ATOM   3179 C  C   . GLY B 1 112 ? -14.275 -5.853  12.516  1.00 21.76 ? 112 GLY B C   1 
ATOM   3180 O  O   . GLY B 1 112 ? -14.258 -6.949  13.068  1.00 24.23 ? 112 GLY B O   1 
ATOM   3181 N  N   . GLU B 1 113 ? -14.440 -5.690  11.193  1.00 24.96 ? 113 GLU B N   1 
ATOM   3182 C  CA  . GLU B 1 113 ? -14.674 -6.847  10.323  1.00 28.63 ? 113 GLU B CA  1 
ATOM   3183 C  C   . GLU B 1 113 ? -13.343 -7.507  9.921   1.00 33.08 ? 113 GLU B C   1 
ATOM   3184 O  O   . GLU B 1 113 ? -13.384 -8.520  9.212   1.00 31.00 ? 113 GLU B O   1 
ATOM   3185 C  CB  . GLU B 1 113 ? -15.363 -6.465  8.999   1.00 35.53 ? 113 GLU B CB  1 
ATOM   3186 C  CG  . GLU B 1 113 ? -16.559 -5.508  9.106   1.00 44.63 ? 113 GLU B CG  1 
ATOM   3187 C  CD  . GLU B 1 113 ? -17.892 -6.220  9.213   1.00 49.03 ? 113 GLU B CD  1 
ATOM   3188 O  OE1 . GLU B 1 113 ? -17.949 -7.131  10.068  1.00 56.63 ? 113 GLU B OE1 1 
ATOM   3189 N  N   . GLY B 1 114 ? -12.167 -6.949  10.342  1.00 22.03 ? 114 GLY B N   1 
ATOM   3190 C  CA  . GLY B 1 114 ? -10.904 -7.674  10.186  1.00 18.90 ? 114 GLY B CA  1 
ATOM   3191 C  C   . GLY B 1 114 ? -9.919  -6.864  9.344   1.00 18.64 ? 114 GLY B C   1 
ATOM   3192 O  O   . GLY B 1 114 ? -10.172 -5.714  9.025   1.00 18.02 ? 114 GLY B O   1 
ATOM   3193 N  N   . ALA B 1 115 ? -8.812  -7.517  8.971   1.00 16.71 ? 115 ALA B N   1 
ATOM   3194 C  CA  . ALA B 1 115 ? -7.668  -6.917  8.295   1.00 16.27 ? 115 ALA B CA  1 
ATOM   3195 C  C   . ALA B 1 115 ? -7.661  -7.204  6.795   1.00 17.99 ? 115 ALA B C   1 
ATOM   3196 O  O   . ALA B 1 115 ? -6.896  -6.581  6.045   1.00 17.82 ? 115 ALA B O   1 
ATOM   3197 C  CB  . ALA B 1 115 ? -6.412  -7.429  8.953   1.00 14.10 ? 115 ALA B CB  1 
ATOM   3198 N  N   . TYR B 1 116 ? -8.516  -8.148  6.366   1.00 19.18 ? 116 TYR B N   1 
ATOM   3199 C  CA  . TYR B 1 116 ? -8.586  -8.476  4.940   1.00 20.21 ? 116 TYR B CA  1 
ATOM   3200 C  C   . TYR B 1 116 ? -9.922  -9.193  4.702   1.00 22.99 ? 116 TYR B C   1 
ATOM   3201 O  O   . TYR B 1 116 ? -10.618 -9.470  5.660   1.00 19.71 ? 116 TYR B O   1 
ATOM   3202 C  CB  . TYR B 1 116 ? -7.348  -9.280  4.513   1.00 20.37 ? 116 TYR B CB  1 
ATOM   3203 C  CG  . TYR B 1 116 ? -7.318  -10.668 5.097   1.00 22.06 ? 116 TYR B CG  1 
ATOM   3204 C  CD1 . TYR B 1 116 ? -6.810  -10.867 6.362   1.00 21.46 ? 116 TYR B CD1 1 
ATOM   3205 C  CD2 . TYR B 1 116 ? -7.849  -11.783 4.430   1.00 22.86 ? 116 TYR B CD2 1 
ATOM   3206 C  CE1 . TYR B 1 116 ? -6.793  -12.125 6.944   1.00 26.35 ? 116 TYR B CE1 1 
ATOM   3207 C  CE2 . TYR B 1 116 ? -7.906  -13.024 5.037   1.00 27.77 ? 116 TYR B CE2 1 
ATOM   3208 C  CZ  . TYR B 1 116 ? -7.370  -13.186 6.299   1.00 27.50 ? 116 TYR B CZ  1 
ATOM   3209 O  OH  . TYR B 1 116 ? -7.315  -14.356 7.032   1.00 37.56 ? 116 TYR B OH  1 
ATOM   3210 N  N   . GLY B 1 117 ? -10.275 -9.454  3.432   1.00 31.44 ? 117 GLY B N   1 
ATOM   3211 C  CA  . GLY B 1 117 ? -11.468 -10.231 3.098   1.00 34.99 ? 117 GLY B CA  1 
ATOM   3212 C  C   . GLY B 1 117 ? -12.756 -9.414  3.138   1.00 34.98 ? 117 GLY B C   1 
ATOM   3213 O  O   . GLY B 1 117 ? -13.819 -9.939  2.847   1.00 37.78 ? 117 GLY B O   1 
ATOM   3214 N  N   . GLY B 1 118 ? -12.662 -8.115  3.433   1.00 33.63 ? 118 GLY B N   1 
ATOM   3215 C  CA  . GLY B 1 118 ? -13.759 -7.184  3.236   1.00 29.26 ? 118 GLY B CA  1 
ATOM   3216 C  C   . GLY B 1 118 ? -13.921 -6.758  1.765   1.00 27.15 ? 118 GLY B C   1 
ATOM   3217 O  O   . GLY B 1 118 ? -13.296 -7.325  0.874   1.00 29.78 ? 118 GLY B O   1 
ATOM   3218 N  N   . LEU B 1 119 ? -14.757 -5.743  1.572   1.00 25.25 ? 119 LEU B N   1 
ATOM   3219 C  CA  . LEU B 1 119 ? -15.006 -5.072  0.315   1.00 25.20 ? 119 LEU B CA  1 
ATOM   3220 C  C   . LEU B 1 119 ? -13.675 -4.548  -0.174  1.00 30.33 ? 119 LEU B C   1 
ATOM   3221 O  O   . LEU B 1 119 ? -12.984 -3.861  0.606   1.00 31.34 ? 119 LEU B O   1 
ATOM   3222 C  CB  . LEU B 1 119 ? -15.943 -3.878  0.566   1.00 30.19 ? 119 LEU B CB  1 
ATOM   3223 N  N   . PRO B 1 120 ? -13.253 -4.890  -1.424  1.00 25.79 ? 120 PRO B N   1 
ATOM   3224 C  CA  . PRO B 1 120 ? -12.024 -4.352  -1.989  1.00 26.18 ? 120 PRO B CA  1 
ATOM   3225 C  C   . PRO B 1 120 ? -11.930 -2.838  -1.909  1.00 23.54 ? 120 PRO B C   1 
ATOM   3226 O  O   . PRO B 1 120 ? -10.825 -2.307  -1.814  1.00 20.73 ? 120 PRO B O   1 
ATOM   3227 C  CB  . PRO B 1 120 ? -12.065 -4.765  -3.479  1.00 31.50 ? 120 PRO B CB  1 
ATOM   3228 C  CG  . PRO B 1 120 ? -12.920 -6.011  -3.504  1.00 32.74 ? 120 PRO B CG  1 
ATOM   3229 C  CD  . PRO B 1 120 ? -13.791 -5.968  -2.265  1.00 30.05 ? 120 PRO B CD  1 
ATOM   3230 N  N   . GLU B 1 121 ? -13.046 -2.115  -2.113  1.00 20.96 ? 121 GLU B N   1 
ATOM   3231 C  CA  . GLU B 1 121 ? -12.944 -0.671  -2.258  1.00 22.84 ? 121 GLU B CA  1 
ATOM   3232 C  C   . GLU B 1 121 ? -12.989 0.069   -0.915  1.00 20.82 ? 121 GLU B C   1 
ATOM   3233 O  O   . GLU B 1 121 ? -12.895 1.287   -0.902  1.00 24.73 ? 121 GLU B O   1 
ATOM   3234 C  CB  . GLU B 1 121 ? -14.093 -0.162  -3.137  1.00 34.85 ? 121 GLU B CB  1 
ATOM   3235 C  CG  . GLU B 1 121 ? -14.148 -0.819  -4.509  1.00 44.92 ? 121 GLU B CG  1 
ATOM   3236 C  CD  . GLU B 1 121 ? -14.807 -2.204  -4.607  1.00 54.71 ? 121 GLU B CD  1 
ATOM   3237 O  OE1 . GLU B 1 121 ? -15.312 -2.753  -3.575  1.00 49.57 ? 121 GLU B OE1 1 
ATOM   3238 O  OE2 . GLU B 1 121 ? -14.807 -2.753  -5.728  1.00 68.20 ? 121 GLU B OE2 1 
ATOM   3239 N  N   . ALA B 1 122 ? -13.048 -0.650  0.216   1.00 18.16 ? 122 ALA B N   1 
ATOM   3240 C  CA  . ALA B 1 122 ? -13.042 -0.027  1.518   1.00 21.18 ? 122 ALA B CA  1 
ATOM   3241 C  C   . ALA B 1 122 ? -11.679 -0.259  2.166   1.00 20.86 ? 122 ALA B C   1 
ATOM   3242 O  O   . ALA B 1 122 ? -11.045 -1.319  1.978   1.00 15.79 ? 122 ALA B O   1 
ATOM   3243 C  CB  . ALA B 1 122 ? -14.078 -0.608  2.415   1.00 24.50 ? 122 ALA B CB  1 
ATOM   3244 N  N   . PRO B 1 123 ? -11.246 0.715   2.974   1.00 20.00 ? 123 PRO B N   1 
ATOM   3245 C  CA  . PRO B 1 123 ? -10.073 0.496   3.836   1.00 21.64 ? 123 PRO B CA  1 
ATOM   3246 C  C   . PRO B 1 123 ? -10.377 -0.624  4.796   1.00 17.60 ? 123 PRO B C   1 
ATOM   3247 O  O   . PRO B 1 123 ? -11.457 -0.731  5.341   1.00 20.88 ? 123 PRO B O   1 
ATOM   3248 C  CB  . PRO B 1 123 ? -9.884  1.806   4.604   1.00 21.73 ? 123 PRO B CB  1 
ATOM   3249 C  CG  . PRO B 1 123 ? -10.742 2.813   3.869   1.00 23.49 ? 123 PRO B CG  1 
ATOM   3250 C  CD  . PRO B 1 123 ? -11.824 2.052   3.144   1.00 21.23 ? 123 PRO B CD  1 
ATOM   3251 N  N   . PRO B 1 124 ? -9.427  -1.519  5.073   1.00 16.10 ? 124 PRO B N   1 
ATOM   3252 C  CA  . PRO B 1 124 ? -9.681  -2.534  6.067   1.00 15.63 ? 124 PRO B CA  1 
ATOM   3253 C  C   . PRO B 1 124 ? -9.886  -1.917  7.459   1.00 15.84 ? 124 PRO B C   1 
ATOM   3254 O  O   . PRO B 1 124 ? -9.245  -0.911  7.797   1.00 15.62 ? 124 PRO B O   1 
ATOM   3255 C  CB  . PRO B 1 124 ? -8.406  -3.356  6.010   1.00 17.69 ? 124 PRO B CB  1 
ATOM   3256 C  CG  . PRO B 1 124 ? -7.378  -2.499  5.390   1.00 20.22 ? 124 PRO B CG  1 
ATOM   3257 C  CD  . PRO B 1 124 ? -8.072  -1.547  4.451   1.00 17.35 ? 124 PRO B CD  1 
ATOM   3258 N  N   . ASP B 1 125 ? -10.702 -2.592  8.288   1.00 17.47 ? 125 ASP B N   1 
ATOM   3259 C  CA  . ASP B 1 125 ? -11.015 -2.078  9.608   1.00 15.85 ? 125 ASP B CA  1 
ATOM   3260 C  C   . ASP B 1 125 ? -9.804  -2.206  10.550  1.00 15.32 ? 125 ASP B C   1 
ATOM   3261 O  O   . ASP B 1 125 ? -9.641  -1.371  11.456  1.00 19.02 ? 125 ASP B O   1 
ATOM   3262 C  CB  . ASP B 1 125 ? -12.155 -2.870  10.238  1.00 18.60 ? 125 ASP B CB  1 
ATOM   3263 C  CG  . ASP B 1 125 ? -13.547 -2.521  9.735   1.00 22.60 ? 125 ASP B CG  1 
ATOM   3264 O  OD1 . ASP B 1 125 ? -13.660 -1.596  8.902   1.00 27.54 ? 125 ASP B OD1 1 
ATOM   3265 O  OD2 . ASP B 1 125 ? -14.477 -3.235  10.187  1.00 25.79 ? 125 ASP B OD2 1 
ATOM   3266 N  N   . ASP B 1 126 ? -8.985  -3.219  10.333  1.00 13.87 ? 126 ASP B N   1 
ATOM   3267 C  CA  . ASP B 1 126 ? -7.792  -3.476  11.133  1.00 13.23 ? 126 ASP B CA  1 
ATOM   3268 C  C   . ASP B 1 126 ? -6.578  -3.360  10.221  1.00 12.82 ? 126 ASP B C   1 
ATOM   3269 O  O   . ASP B 1 126 ? -6.618  -3.737  9.048   1.00 12.73 ? 126 ASP B O   1 
ATOM   3270 C  CB  . ASP B 1 126 ? -7.791  -4.864  11.757  1.00 13.49 ? 126 ASP B CB  1 
ATOM   3271 C  CG  . ASP B 1 126 ? -6.692  -5.079  12.787  1.00 15.15 ? 126 ASP B CG  1 
ATOM   3272 O  OD1 . ASP B 1 126 ? -5.504  -5.125  12.418  1.00 13.64 ? 126 ASP B OD1 1 
ATOM   3273 O  OD2 . ASP B 1 126 ? -7.005  -5.209  13.981  1.00 14.52 ? 126 ASP B OD2 1 
ATOM   3274 N  N   . THR B 1 127 ? -5.520  -2.670  10.710  1.00 14.34 ? 127 THR B N   1 
ATOM   3275 C  CA  . THR B 1 127 ? -4.372  -2.351  9.861   1.00 11.57 ? 127 THR B CA  1 
ATOM   3276 C  C   . THR B 1 127 ? -3.471  -3.552  9.571   1.00 12.12 ? 127 THR B C   1 
ATOM   3277 O  O   . THR B 1 127 ? -2.633  -3.470  8.654   1.00 12.57 ? 127 THR B O   1 
ATOM   3278 C  CB  . THR B 1 127 ? -3.646  -1.133  10.425  1.00 13.23 ? 127 THR B CB  1 
ATOM   3279 O  OG1 . THR B 1 127 ? -3.094  -1.482  11.695  1.00 12.87 ? 127 THR B OG1 1 
ATOM   3280 C  CG2 . THR B 1 127 ? -4.604  0.043   10.472  1.00 14.06 ? 127 THR B CG2 1 
ATOM   3281 N  N   . GLY B 1 128 ? -3.660  -4.702  10.227  1.00 13.00 ? 128 GLY B N   1 
ATOM   3282 C  CA  . GLY B 1 128 ? -3.116  -5.977  9.781   1.00 12.43 ? 128 GLY B CA  1 
ATOM   3283 C  C   . GLY B 1 128 ? -1.751  -6.383  10.293  1.00 12.02 ? 128 GLY B C   1 
ATOM   3284 O  O   . GLY B 1 128 ? -1.422  -7.519  10.136  1.00 14.58 ? 128 GLY B O   1 
ATOM   3285 N  N   . GLU B 1 129 ? -0.981  -5.518  11.012  1.00 12.37 ? 129 GLU B N   1 
ATOM   3286 C  CA  . GLU B 1 129 ? 0.381   -5.871  11.392  1.00 11.41 ? 129 GLU B CA  1 
ATOM   3287 C  C   . GLU B 1 129 ? 0.468   -6.865  12.563  1.00 11.79 ? 129 GLU B C   1 
ATOM   3288 O  O   . GLU B 1 129 ? 1.554   -7.323  12.842  1.00 13.65 ? 129 GLU B O   1 
ATOM   3289 C  CB  . GLU B 1 129 ? 1.182   -4.591  11.628  1.00 13.18 ? 129 GLU B CB  1 
ATOM   3290 C  CG  . GLU B 1 129 ? 0.871   -3.843  12.930  1.00 13.19 ? 129 GLU B CG  1 
ATOM   3291 C  CD  . GLU B 1 129 ? -0.147  -2.741  12.751  1.00 13.80 ? 129 GLU B CD  1 
ATOM   3292 O  OE1 . GLU B 1 129 ? -0.990  -2.860  11.829  1.00 13.52 ? 129 GLU B OE1 1 
ATOM   3293 O  OE2 . GLU B 1 129 ? -0.139  -1.778  13.540  1.00 14.12 ? 129 GLU B OE2 1 
ATOM   3294 N  N   . ALA B 1 130 ? -0.640  -7.188  13.236  1.00 10.94 ? 130 ALA B N   1 
ATOM   3295 C  CA  . ALA B 1 130 ? -0.673  -8.204  14.248  1.00 12.89 ? 130 ALA B CA  1 
ATOM   3296 C  C   . ALA B 1 130 ? -1.191  -9.554  13.725  1.00 12.87 ? 130 ALA B C   1 
ATOM   3297 O  O   . ALA B 1 130 ? -1.282  -10.520 14.519  1.00 14.73 ? 130 ALA B O   1 
ATOM   3298 C  CB  . ALA B 1 130 ? -1.473  -7.740  15.473  1.00 15.97 ? 130 ALA B CB  1 
ATOM   3299 N  N   . LEU B 1 131 ? -1.533  -9.680  12.449  1.00 14.42 ? 131 LEU B N   1 
ATOM   3300 C  CA  . LEU B 1 131 ? -1.981  -10.979 11.954  1.00 14.35 ? 131 LEU B CA  1 
ATOM   3301 C  C   . LEU B 1 131 ? -0.898  -12.008 12.198  1.00 15.70 ? 131 LEU B C   1 
ATOM   3302 O  O   . LEU B 1 131 ? 0.255   -11.763 11.925  1.00 18.17 ? 131 LEU B O   1 
ATOM   3303 C  CB  . LEU B 1 131 ? -2.280  -10.947 10.473  1.00 14.03 ? 131 LEU B CB  1 
ATOM   3304 C  CG  . LEU B 1 131 ? -3.572  -10.227 10.129  1.00 18.16 ? 131 LEU B CG  1 
ATOM   3305 C  CD1 . LEU B 1 131 ? -3.596  -9.919  8.655   1.00 21.60 ? 131 LEU B CD1 1 
ATOM   3306 C  CD2 . LEU B 1 131 ? -4.818  -11.046 10.581  1.00 19.21 ? 131 LEU B CD2 1 
ATOM   3307 N  N   . GLY B 1 132 ? -1.322  -13.161 12.653  1.00 19.31 ? 132 GLY B N   1 
ATOM   3308 C  CA  . GLY B 1 132 ? -0.436  -14.272 12.917  1.00 18.44 ? 132 GLY B CA  1 
ATOM   3309 C  C   . GLY B 1 132 ? 0.265   -14.220 14.267  1.00 20.45 ? 132 GLY B C   1 
ATOM   3310 O  O   . GLY B 1 132 ? 1.006   -15.148 14.559  1.00 19.35 ? 132 GLY B O   1 
ATOM   3311 N  N   . LEU B 1 133 ? 0.038   -13.154 15.054  1.00 18.87 ? 133 LEU B N   1 
ATOM   3312 C  CA  . LEU B 1 133 ? 0.652   -13.043 16.368  1.00 16.26 ? 133 LEU B CA  1 
ATOM   3313 C  C   . LEU B 1 133 ? -0.341  -13.572 17.392  1.00 16.79 ? 133 LEU B C   1 
ATOM   3314 O  O   . LEU B 1 133 ? -1.515  -13.674 17.191  1.00 22.16 ? 133 LEU B O   1 
ATOM   3315 C  CB  . LEU B 1 133 ? 1.056   -11.586 16.616  1.00 17.03 ? 133 LEU B CB  1 
ATOM   3316 C  CG  . LEU B 1 133 ? 2.029   -11.010 15.584  1.00 17.75 ? 133 LEU B CG  1 
ATOM   3317 C  CD1 . LEU B 1 133 ? 2.456   -9.632  15.986  1.00 17.79 ? 133 LEU B CD1 1 
ATOM   3318 C  CD2 . LEU B 1 133 ? 3.243   -11.910 15.399  1.00 17.01 ? 133 LEU B CD2 1 
ATOM   3319 N  N   . LYS B 1 134 ? 0.164   -13.817 18.590  1.00 19.78 ? 134 LYS B N   1 
ATOM   3320 C  CA  . LYS B 1 134 ? -0.677  -14.353 19.662  1.00 18.87 ? 134 LYS B CA  1 
ATOM   3321 C  C   . LYS B 1 134 ? -1.192  -13.150 20.454  1.00 15.34 ? 134 LYS B C   1 
ATOM   3322 O  O   . LYS B 1 134 ? -0.674  -12.044 20.328  1.00 15.74 ? 134 LYS B O   1 
ATOM   3323 C  CB  . LYS B 1 134 ? 0.230   -15.293 20.485  1.00 22.68 ? 134 LYS B CB  1 
ATOM   3324 C  CG  . LYS B 1 134 ? 0.684   -16.520 19.660  1.00 28.36 ? 134 LYS B CG  1 
ATOM   3325 C  CD  . LYS B 1 134 ? 1.322   -17.659 20.450  1.00 33.92 ? 134 LYS B CD  1 
ATOM   3326 N  N   . PRO B 1 135 ? -2.129  -13.355 21.389  1.00 15.32 ? 135 PRO B N   1 
ATOM   3327 C  CA  . PRO B 1 135 ? -2.579  -12.210 22.199  1.00 16.74 ? 135 PRO B CA  1 
ATOM   3328 C  C   . PRO B 1 135 ? -1.461  -11.635 23.035  1.00 14.62 ? 135 PRO B C   1 
ATOM   3329 O  O   . PRO B 1 135 ? -1.508  -10.456 23.378  1.00 16.13 ? 135 PRO B O   1 
ATOM   3330 C  CB  . PRO B 1 135 ? -3.701  -12.760 23.109  1.00 19.24 ? 135 PRO B CB  1 
ATOM   3331 C  CG  . PRO B 1 135 ? -4.073  -14.079 22.465  1.00 19.02 ? 135 PRO B CG  1 
ATOM   3332 C  CD  . PRO B 1 135 ? -2.865  -14.591 21.659  1.00 15.88 ? 135 PRO B CD  1 
ATOM   3333 N  N   A SER B 1 136 ? -0.485  -12.452 23.432  0.45 13.61 ? 136 SER B N   1 
ATOM   3334 N  N   B SER B 1 136 ? -0.527  -12.492 23.458  0.55 14.26 ? 136 SER B N   1 
ATOM   3335 C  CA  A SER B 1 136 ? 0.728   -11.911 24.033  0.45 12.87 ? 136 SER B CA  1 
ATOM   3336 C  CA  B SER B 1 136 ? 0.706   -12.026 24.076  0.55 14.00 ? 136 SER B CA  1 
ATOM   3337 C  C   A SER B 1 136 ? 0.480   -11.290 25.412  0.45 12.28 ? 136 SER B C   1 
ATOM   3338 C  C   B SER B 1 136 ? 0.418   -11.252 25.367  0.55 12.70 ? 136 SER B C   1 
ATOM   3339 O  O   A SER B 1 136 ? 1.250   -10.405 25.801  0.45 12.42 ? 136 SER B O   1 
ATOM   3340 O  O   B SER B 1 136 ? 1.084   -10.256 25.663  0.55 12.60 ? 136 SER B O   1 
ATOM   3341 C  CB  A SER B 1 136 ? 1.334   -10.841 23.125  0.45 12.90 ? 136 SER B CB  1 
ATOM   3342 C  CB  B SER B 1 136 ? 1.517   -11.182 23.095  0.55 15.91 ? 136 SER B CB  1 
ATOM   3343 O  OG  A SER B 1 136 ? 2.741   -10.839 23.264  0.45 13.22 ? 136 SER B OG  1 
ATOM   3344 O  OG  B SER B 1 136 ? 2.168   -12.017 22.133  0.55 17.67 ? 136 SER B OG  1 
ATOM   3345 N  N   . ARG B 1 137 ? -0.583  -11.706 26.108  1.00 11.86 ? 137 ARG B N   1 
ATOM   3346 C  CA  . ARG B 1 137 ? -0.945  -11.162 27.407  1.00 11.68 ? 137 ARG B CA  1 
ATOM   3347 C  C   . ARG B 1 137 ? -1.213  -9.656  27.314  1.00 13.24 ? 137 ARG B C   1 
ATOM   3348 O  O   . ARG B 1 137 ? -1.013  -8.945  28.274  1.00 13.25 ? 137 ARG B O   1 
ATOM   3349 C  CB  . ARG B 1 137 ? 0.125   -11.384 28.489  1.00 12.63 ? 137 ARG B CB  1 
ATOM   3350 C  CG  . ARG B 1 137 ? 0.350   -12.880 28.787  1.00 13.12 ? 137 ARG B CG  1 
ATOM   3351 C  CD  . ARG B 1 137 ? 1.091   -13.096 30.071  1.00 13.75 ? 137 ARG B CD  1 
ATOM   3352 N  NE  . ARG B 1 137 ? 2.451   -12.593 29.915  1.00 14.58 ? 137 ARG B NE  1 
ATOM   3353 C  CZ  . ARG B 1 137 ? 3.314   -12.390 30.910  1.00 15.25 ? 137 ARG B CZ  1 
ATOM   3354 N  NH1 . ARG B 1 137 ? 4.496   -11.819 30.710  1.00 14.42 ? 137 ARG B NH1 1 
ATOM   3355 N  NH2 . ARG B 1 137 ? 2.964   -12.800 32.116  1.00 16.97 ? 137 ARG B NH2 1 
ATOM   3356 N  N   . LEU B 1 138 ? -1.715  -9.204  26.149  1.00 10.80 ? 138 LEU B N   1 
ATOM   3357 C  CA  . LEU B 1 138 ? -2.032  -7.798  25.993  1.00 11.23 ? 138 LEU B CA  1 
ATOM   3358 C  C   . LEU B 1 138 ? -3.042  -7.343  27.017  1.00 11.99 ? 138 LEU B C   1 
ATOM   3359 O  O   . LEU B 1 138 ? -4.124  -7.927  27.137  1.00 12.27 ? 138 LEU B O   1 
ATOM   3360 C  CB  . LEU B 1 138 ? -2.558  -7.530  24.583  1.00 11.73 ? 138 LEU B CB  1 
ATOM   3361 C  CG  . LEU B 1 138 ? -2.992  -6.096  24.301  1.00 12.36 ? 138 LEU B CG  1 
ATOM   3362 C  CD1 . LEU B 1 138 ? -1.804  -5.168  24.251  1.00 13.66 ? 138 LEU B CD1 1 
ATOM   3363 C  CD2 . LEU B 1 138 ? -3.841  -6.008  23.022  1.00 14.59 ? 138 LEU B CD2 1 
ATOM   3364 N  N   . THR B 1 139 ? -2.726  -6.206  27.668  1.00 10.30 ? 139 THR B N   1 
ATOM   3365 C  CA  . THR B 1 139 ? -3.725  -5.500  28.453  1.00 10.58 ? 139 THR B CA  1 
ATOM   3366 C  C   . THR B 1 139 ? -3.741  -4.060  27.939  1.00 10.21 ? 139 THR B C   1 
ATOM   3367 O  O   . THR B 1 139 ? -2.744  -3.559  27.419  1.00 10.15 ? 139 THR B O   1 
ATOM   3368 C  CB  . THR B 1 139 ? -3.450  -5.552  29.948  1.00 11.11 ? 139 THR B CB  1 
ATOM   3369 O  OG1 . THR B 1 139 ? -2.165  -5.027  30.236  1.00 11.69 ? 139 THR B OG1 1 
ATOM   3370 C  CG2 . THR B 1 139 ? -3.517  -6.982  30.448  1.00 11.85 ? 139 THR B CG2 1 
ATOM   3371 N  N   . LEU B 1 140 ? -4.933  -3.469  27.936  1.00 9.94  ? 140 LEU B N   1 
ATOM   3372 C  CA  . LEU B 1 140 ? -5.144  -2.078  27.552  1.00 10.74 ? 140 LEU B CA  1 
ATOM   3373 C  C   . LEU B 1 140 ? -5.852  -1.418  28.712  1.00 10.17 ? 140 LEU B C   1 
ATOM   3374 O  O   . LEU B 1 140 ? -6.930  -1.848  29.138  1.00 11.65 ? 140 LEU B O   1 
ATOM   3375 C  CB  . LEU B 1 140 ? -6.041  -2.043  26.311  1.00 12.83 ? 140 LEU B CB  1 
ATOM   3376 C  CG  . LEU B 1 140 ? -5.376  -2.617  25.050  1.00 12.35 ? 140 LEU B CG  1 
ATOM   3377 C  CD1 . LEU B 1 140 ? -6.386  -2.711  23.913  1.00 14.44 ? 140 LEU B CD1 1 
ATOM   3378 C  CD2 . LEU B 1 140 ? -4.219  -1.762  24.653  1.00 13.91 ? 140 LEU B CD2 1 
ATOM   3379 N  N   . THR B 1 141 ? -5.182  -0.383  29.253  1.00 10.50 ? 141 THR B N   1 
ATOM   3380 C  CA  . THR B 1 141 ? -5.692  0.298   30.443  1.00 11.45 ? 141 THR B CA  1 
ATOM   3381 C  C   . THR B 1 141 ? -5.863  1.770   30.059  1.00 11.28 ? 141 THR B C   1 
ATOM   3382 O  O   . THR B 1 141 ? -4.887  2.405   29.641  1.00 10.81 ? 141 THR B O   1 
ATOM   3383 C  CB  . THR B 1 141 ? -4.680  0.169   31.595  1.00 11.74 ? 141 THR B CB  1 
ATOM   3384 O  OG1 . THR B 1 141 ? -4.290  -1.219  31.692  1.00 13.65 ? 141 THR B OG1 1 
ATOM   3385 C  CG2 . THR B 1 141 ? -5.210  0.680   32.918  1.00 13.22 ? 141 THR B CG2 1 
ATOM   3386 N  N   . ILE B 1 142 ? -7.068  2.275   30.282  1.00 11.12 ? 142 ILE B N   1 
ATOM   3387 C  CA  . ILE B 1 142 ? -7.365  3.659   29.917  1.00 12.34 ? 142 ILE B CA  1 
ATOM   3388 C  C   . ILE B 1 142 ? -7.321  4.510   31.189  1.00 12.49 ? 142 ILE B C   1 
ATOM   3389 O  O   . ILE B 1 142 ? -7.701  4.064   32.261  1.00 10.31 ? 142 ILE B O   1 
ATOM   3390 C  CB  . ILE B 1 142 ? -8.708  3.787   29.197  1.00 13.17 ? 142 ILE B CB  1 
ATOM   3391 C  CG1 . ILE B 1 142 ? -8.808  5.188   28.567  1.00 13.35 ? 142 ILE B CG1 1 
ATOM   3392 C  CG2 . ILE B 1 142 ? -9.887  3.411   30.107  1.00 13.34 ? 142 ILE B CG2 1 
ATOM   3393 C  CD1 . ILE B 1 142 ? -9.931  5.267   27.551  1.00 14.52 ? 142 ILE B CD1 1 
ATOM   3394 N  N   . GLY B 1 143 ? -6.885  5.778   31.053  1.00 11.30 ? 143 GLY B N   1 
ATOM   3395 C  CA  . GLY B 1 143 ? -6.953  6.747   32.132  1.00 10.91 ? 143 GLY B CA  1 
ATOM   3396 C  C   . GLY B 1 143 ? -7.357  8.127   31.590  1.00 11.89 ? 143 GLY B C   1 
ATOM   3397 O  O   . GLY B 1 143 ? -7.182  8.443   30.405  1.00 10.97 ? 143 GLY B O   1 
ATOM   3398 N  N   . PHE B 1 144 ? -7.868  8.971   32.508  1.00 11.37 ? 144 PHE B N   1 
ATOM   3399 C  CA  . PHE B 1 144 ? -8.413  10.310  32.187  1.00 11.46 ? 144 PHE B CA  1 
ATOM   3400 C  C   . PHE B 1 144 ? -7.598  11.350  32.928  1.00 9.98  ? 144 PHE B C   1 
ATOM   3401 O  O   . PHE B 1 144 ? -7.378  11.259  34.171  1.00 10.99 ? 144 PHE B O   1 
ATOM   3402 C  CB  . PHE B 1 144 ? -9.857  10.416  32.662  1.00 13.13 ? 144 PHE B CB  1 
ATOM   3403 C  CG  . PHE B 1 144 ? -10.808 9.398   32.058  1.00 15.23 ? 144 PHE B CG  1 
ATOM   3404 C  CD1 . PHE B 1 144 ? -10.681 9.018   30.728  1.00 19.51 ? 144 PHE B CD1 1 
ATOM   3405 C  CD2 . PHE B 1 144 ? -11.898 8.906   32.787  1.00 16.95 ? 144 PHE B CD2 1 
ATOM   3406 C  CE1 . PHE B 1 144 ? -11.581 8.112   30.153  1.00 18.95 ? 144 PHE B CE1 1 
ATOM   3407 C  CE2 . PHE B 1 144 ? -12.768 7.994   32.211  1.00 15.14 ? 144 PHE B CE2 1 
ATOM   3408 C  CZ  . PHE B 1 144 ? -12.634 7.634   30.887  1.00 16.11 ? 144 PHE B CZ  1 
ATOM   3409 N  N   . GLY B 1 145 ? -7.048  12.294  32.167  1.00 12.63 ? 145 GLY B N   1 
ATOM   3410 C  CA  . GLY B 1 145 ? -6.221  13.350  32.731  1.00 10.93 ? 145 GLY B CA  1 
ATOM   3411 C  C   . GLY B 1 145 ? -7.061  14.496  33.258  1.00 14.98 ? 145 GLY B C   1 
ATOM   3412 O  O   . GLY B 1 145 ? -8.226  14.652  32.911  1.00 12.17 ? 145 GLY B O   1 
ATOM   3413 N  N   . PRO B 1 146 ? -6.481  15.329  34.133  1.00 14.85 ? 146 PRO B N   1 
ATOM   3414 C  CA  . PRO B 1 146 ? -7.222  16.439  34.718  1.00 15.53 ? 146 PRO B CA  1 
ATOM   3415 C  C   . PRO B 1 146 ? -7.840  17.384  33.711  1.00 14.45 ? 146 PRO B C   1 
ATOM   3416 O  O   . PRO B 1 146 ? -8.945  17.876  33.912  1.00 17.11 ? 146 PRO B O   1 
ATOM   3417 C  CB  . PRO B 1 146 ? -6.147  17.236  35.483  1.00 16.15 ? 146 PRO B CB  1 
ATOM   3418 C  CG  . PRO B 1 146 ? -5.008  16.270  35.728  1.00 18.36 ? 146 PRO B CG  1 
ATOM   3419 C  CD  . PRO B 1 146 ? -5.148  15.160  34.724  1.00 16.73 ? 146 PRO B CD  1 
ATOM   3420 N  N   . SER B 1 147 ? -7.172  17.540  32.562  1.00 13.53 ? 147 SER B N   1 
ATOM   3421 C  CA  . SER B 1 147 ? -7.636  18.421  31.486  1.00 15.25 ? 147 SER B CA  1 
ATOM   3422 C  C   . SER B 1 147 ? -8.915  17.902  30.809  1.00 17.86 ? 147 SER B C   1 
ATOM   3423 O  O   . SER B 1 147 ? -9.690  18.688  30.299  1.00 16.41 ? 147 SER B O   1 
ATOM   3424 C  CB  . SER B 1 147 ? -6.475  18.662  30.522  1.00 16.35 ? 147 SER B CB  1 
ATOM   3425 O  OG  . SER B 1 147 ? -6.066  17.387  29.963  1.00 16.23 ? 147 SER B OG  1 
ATOM   3426 N  N   . LEU B 1 148 ? -9.233  16.582  30.930  1.00 13.25 ? 148 LEU B N   1 
ATOM   3427 C  CA  . LEU B 1 148 ? -10.458 16.091  30.337  1.00 13.45 ? 148 LEU B CA  1 
ATOM   3428 C  C   . LEU B 1 148 ? -11.655 16.729  31.036  1.00 15.03 ? 148 LEU B C   1 
ATOM   3429 O  O   . LEU B 1 148 ? -12.733 16.841  30.450  1.00 15.68 ? 148 LEU B O   1 
ATOM   3430 C  CB  . LEU B 1 148 ? -10.557 14.568  30.522  1.00 15.55 ? 148 LEU B CB  1 
ATOM   3431 C  CG  . LEU B 1 148 ? -11.736 13.915  29.803  1.00 19.08 ? 148 LEU B CG  1 
ATOM   3432 C  CD1 . LEU B 1 148 ? -11.578 14.085  28.330  1.00 23.93 ? 148 LEU B CD1 1 
ATOM   3433 C  CD2 . LEU B 1 148 ? -11.797 12.460  30.152  1.00 22.62 ? 148 LEU B CD2 1 
ATOM   3434 N  N   . PHE B 1 149 ? -11.481 16.996  32.329  1.00 15.73 ? 149 PHE B N   1 
ATOM   3435 C  CA  . PHE B 1 149 ? -12.608 17.401  33.170  1.00 18.81 ? 149 PHE B CA  1 
ATOM   3436 C  C   . PHE B 1 149 ? -13.042 18.845  32.900  1.00 19.51 ? 149 PHE B C   1 
ATOM   3437 O  O   . PHE B 1 149 ? -14.144 19.199  33.279  1.00 24.69 ? 149 PHE B O   1 
ATOM   3438 C  CB  . PHE B 1 149 ? -12.275 17.174  34.652  1.00 18.92 ? 149 PHE B CB  1 
ATOM   3439 C  CG  . PHE B 1 149 ? -12.113 15.707  34.959  1.00 16.55 ? 149 PHE B CG  1 
ATOM   3440 C  CD1 . PHE B 1 149 ? -10.896 15.069  34.805  1.00 16.98 ? 149 PHE B CD1 1 
ATOM   3441 C  CD2 . PHE B 1 149 ? -13.207 14.979  35.377  1.00 13.98 ? 149 PHE B CD2 1 
ATOM   3442 C  CE1 . PHE B 1 149 ? -10.787 13.698  35.000  1.00 14.08 ? 149 PHE B CE1 1 
ATOM   3443 C  CE2 . PHE B 1 149 ? -13.114 13.616  35.538  1.00 15.45 ? 149 PHE B CE2 1 
ATOM   3444 C  CZ  . PHE B 1 149 ? -11.909 12.989  35.374  1.00 15.04 ? 149 PHE B CZ  1 
ATOM   3445 N  N   . THR B 1 150 ? -12.269 19.588  32.149  1.00 17.15 ? 150 THR B N   1 
ATOM   3446 C  CA  . THR B 1 150 ? -12.692 20.909  31.700  1.00 18.69 ? 150 THR B CA  1 
ATOM   3447 C  C   . THR B 1 150 ? -13.601 20.808  30.467  1.00 22.23 ? 150 THR B C   1 
ATOM   3448 O  O   . THR B 1 150 ? -14.161 21.814  30.047  1.00 21.57 ? 150 THR B O   1 
ATOM   3449 C  CB  . THR B 1 150 ? -11.453 21.773  31.439  1.00 21.56 ? 150 THR B CB  1 
ATOM   3450 O  OG1 . THR B 1 150 ? -10.901 21.354  30.162  1.00 21.48 ? 150 THR B OG1 1 
ATOM   3451 C  CG2 . THR B 1 150 ? -10.390 21.767  32.511  1.00 23.96 ? 150 THR B CG2 1 
ATOM   3452 N  N   . ARG B 1 151 ? -13.868 19.600  29.945  1.00 19.15 ? 151 ARG B N   1 
ATOM   3453 C  CA  . ARG B 1 151 ? -14.742 19.375  28.813  1.00 18.47 ? 151 ARG B CA  1 
ATOM   3454 C  C   . ARG B 1 151 ? -15.979 18.653  29.301  1.00 16.36 ? 151 ARG B C   1 
ATOM   3455 O  O   . ARG B 1 151 ? -16.004 18.069  30.397  1.00 21.03 ? 151 ARG B O   1 
ATOM   3456 C  CB  . ARG B 1 151 ? -14.078 18.482  27.760  1.00 18.01 ? 151 ARG B CB  1 
ATOM   3457 C  CG  . ARG B 1 151 ? -12.849 19.116  27.126  1.00 25.14 ? 151 ARG B CG  1 
ATOM   3458 C  CD  . ARG B 1 151 ? -12.538 18.293  25.887  1.00 28.48 ? 151 ARG B CD  1 
ATOM   3459 N  NE  . ARG B 1 151 ? -11.380 18.898  25.232  1.00 30.82 ? 151 ARG B NE  1 
ATOM   3460 C  CZ  . ARG B 1 151 ? -11.477 19.695  24.188  1.00 31.20 ? 151 ARG B CZ  1 
ATOM   3461 N  NH1 . ARG B 1 151 ? -12.557 19.612  23.413  1.00 27.83 ? 151 ARG B NH1 1 
ATOM   3462 N  NH2 . ARG B 1 151 ? -10.521 20.576  23.956  1.00 33.45 ? 151 ARG B NH2 1 
ATOM   3463 N  N   . PHE B 1 152 ? -17.006 18.675  28.456  1.00 17.91 ? 152 PHE B N   1 
ATOM   3464 C  CA  . PHE B 1 152 ? -18.162 17.826  28.594  1.00 21.53 ? 152 PHE B CA  1 
ATOM   3465 C  C   . PHE B 1 152 ? -18.934 18.108  29.871  1.00 21.39 ? 152 PHE B C   1 
ATOM   3466 O  O   . PHE B 1 152 ? -19.728 17.257  30.267  1.00 25.78 ? 152 PHE B O   1 
ATOM   3467 C  CB  . PHE B 1 152 ? -17.765 16.324  28.521  1.00 21.11 ? 152 PHE B CB  1 
ATOM   3468 C  CG  . PHE B 1 152 ? -16.900 15.986  27.338  1.00 22.11 ? 152 PHE B CG  1 
ATOM   3469 C  CD1 . PHE B 1 152 ? -17.172 16.479  26.079  1.00 21.20 ? 152 PHE B CD1 1 
ATOM   3470 C  CD2 . PHE B 1 152 ? -15.794 15.164  27.479  1.00 21.63 ? 152 PHE B CD2 1 
ATOM   3471 C  CE1 . PHE B 1 152 ? -16.359 16.182  24.993  1.00 18.77 ? 152 PHE B CE1 1 
ATOM   3472 C  CE2 . PHE B 1 152 ? -14.951 14.909  26.401  1.00 19.99 ? 152 PHE B CE2 1 
ATOM   3473 C  CZ  . PHE B 1 152 ? -15.279 15.343  25.148  1.00 17.47 ? 152 PHE B CZ  1 
ATOM   3474 N  N   . GLY B 1 153 ? -18.678 19.238  30.530  1.00 22.49 ? 153 GLY B N   1 
ATOM   3475 C  CA  . GLY B 1 153 ? -19.326 19.589  31.788  1.00 24.04 ? 153 GLY B CA  1 
ATOM   3476 C  C   . GLY B 1 153 ? -18.907 18.702  32.944  1.00 25.56 ? 153 GLY B C   1 
ATOM   3477 O  O   . GLY B 1 153 ? -19.678 18.527  33.874  1.00 26.98 ? 153 GLY B O   1 
ATOM   3478 N  N   . LEU B 1 154 ? -17.645 18.209  32.929  1.00 19.15 ? 154 LEU B N   1 
ATOM   3479 C  CA  . LEU B 1 154 ? -17.256 17.270  33.943  1.00 20.38 ? 154 LEU B CA  1 
ATOM   3480 C  C   . LEU B 1 154 ? -16.518 17.948  35.108  1.00 14.73 ? 154 LEU B C   1 
ATOM   3481 O  O   . LEU B 1 154 ? -15.976 17.207  35.922  1.00 16.23 ? 154 LEU B O   1 
ATOM   3482 C  CB  . LEU B 1 154 ? -16.304 16.236  33.298  1.00 19.14 ? 154 LEU B CB  1 
ATOM   3483 C  CG  . LEU B 1 154 ? -16.881 15.291  32.255  1.00 21.50 ? 154 LEU B CG  1 
ATOM   3484 C  CD1 . LEU B 1 154 ? -15.733 14.483  31.664  1.00 21.59 ? 154 LEU B CD1 1 
ATOM   3485 C  CD2 . LEU B 1 154 ? -17.988 14.379  32.835  1.00 25.32 ? 154 LEU B CD2 1 
ATOM   3486 N  N   . ALA B 1 155 ? -16.447 19.299  35.187  1.00 17.29 ? 155 ALA B N   1 
ATOM   3487 C  CA  . ALA B 1 155 ? -15.521 19.950  36.117  1.00 17.40 ? 155 ALA B CA  1 
ATOM   3488 C  C   . ALA B 1 155 ? -15.720 19.526  37.588  1.00 19.90 ? 155 ALA B C   1 
ATOM   3489 O  O   . ALA B 1 155 ? -14.786 19.325  38.361  1.00 21.18 ? 155 ALA B O   1 
ATOM   3490 C  CB  . ALA B 1 155 ? -15.603 21.461  35.978  1.00 20.27 ? 155 ALA B CB  1 
ATOM   3491 N  N   . ASP B 1 156 ? -16.975 19.346  37.991  1.00 16.96 ? 156 ASP B N   1 
ATOM   3492 C  CA  . ASP B 1 156 ? -17.300 18.937  39.329  1.00 16.27 ? 156 ASP B CA  1 
ATOM   3493 C  C   . ASP B 1 156 ? -17.189 17.446  39.594  1.00 18.17 ? 156 ASP B C   1 
ATOM   3494 O  O   . ASP B 1 156 ? -17.450 17.030  40.700  1.00 18.15 ? 156 ASP B O   1 
ATOM   3495 C  CB  . ASP B 1 156 ? -18.722 19.384  39.687  1.00 17.45 ? 156 ASP B CB  1 
ATOM   3496 C  CG  . ASP B 1 156 ? -19.829 18.888  38.792  1.00 19.07 ? 156 ASP B CG  1 
ATOM   3497 O  OD1 . ASP B 1 156 ? -19.534 18.301  37.752  1.00 22.44 ? 156 ASP B OD1 1 
ATOM   3498 O  OD2 . ASP B 1 156 ? -20.981 19.278  39.032  1.00 21.12 ? 156 ASP B OD2 1 
ATOM   3499 N  N   . LEU B 1 157 ? -16.772 16.657  38.607  1.00 14.26 ? 157 LEU B N   1 
ATOM   3500 C  CA  . LEU B 1 157 ? -16.568 15.226  38.819  1.00 15.38 ? 157 LEU B CA  1 
ATOM   3501 C  C   . LEU B 1 157 ? -15.094 14.853  38.826  1.00 16.38 ? 157 LEU B C   1 
ATOM   3502 O  O   . LEU B 1 157 ? -14.752 13.690  38.977  1.00 17.03 ? 157 LEU B O   1 
ATOM   3503 C  CB  . LEU B 1 157 ? -17.308 14.494  37.706  1.00 16.50 ? 157 LEU B CB  1 
ATOM   3504 C  CG  . LEU B 1 157 ? -18.818 14.484  37.881  1.00 20.29 ? 157 LEU B CG  1 
ATOM   3505 C  CD1 . LEU B 1 157 ? -19.511 13.949  36.630  1.00 23.79 ? 157 LEU B CD1 1 
ATOM   3506 C  CD2 . LEU B 1 157 ? -19.121 13.646  39.084  1.00 24.65 ? 157 LEU B CD2 1 
ATOM   3507 N  N   . ARG B 1 158 ? -14.209 15.856  38.657  1.00 14.24 ? 158 ARG B N   1 
ATOM   3508 C  CA  . ARG B 1 158 ? -12.810 15.613  38.923  1.00 14.46 ? 158 ARG B CA  1 
ATOM   3509 C  C   . ARG B 1 158 ? -12.549 15.122  40.340  1.00 17.43 ? 158 ARG B C   1 
ATOM   3510 O  O   . ARG B 1 158 ? -12.844 15.774  41.350  1.00 16.89 ? 158 ARG B O   1 
ATOM   3511 C  CB  . ARG B 1 158 ? -11.993 16.821  38.544  1.00 16.06 ? 158 ARG B CB  1 
ATOM   3512 C  CG  . ARG B 1 158 ? -10.513 16.547  38.794  1.00 18.75 ? 158 ARG B CG  1 
ATOM   3513 C  CD  . ARG B 1 158 ? -9.731  17.780  38.509  1.00 19.09 ? 158 ARG B CD  1 
ATOM   3514 N  NE  . ARG B 1 158 ? -8.336  17.564  38.930  1.00 21.70 ? 158 ARG B NE  1 
ATOM   3515 C  CZ  . ARG B 1 158 ? -7.390  18.403  38.601  1.00 17.25 ? 158 ARG B CZ  1 
ATOM   3516 N  NH1 . ARG B 1 158 ? -7.723  19.486  37.941  1.00 15.30 ? 158 ARG B NH1 1 
ATOM   3517 N  NH2 . ARG B 1 158 ? -6.183  18.175  39.078  1.00 17.07 ? 158 ARG B NH2 1 
ATOM   3518 N  N   . PRO B 1 159 ? -11.949 13.914  40.504  1.00 16.04 ? 159 PRO B N   1 
ATOM   3519 C  CA  . PRO B 1 159 ? -11.618 13.440  41.838  1.00 15.77 ? 159 PRO B CA  1 
ATOM   3520 C  C   . PRO B 1 159 ? -10.630 14.379  42.541  1.00 14.40 ? 159 PRO B C   1 
ATOM   3521 O  O   . PRO B 1 159 ? -9.633  14.829  41.933  1.00 12.78 ? 159 PRO B O   1 
ATOM   3522 C  CB  . PRO B 1 159 ? -11.051 12.035  41.619  1.00 16.36 ? 159 PRO B CB  1 
ATOM   3523 C  CG  . PRO B 1 159 ? -11.403 11.688  40.185  1.00 17.18 ? 159 PRO B CG  1 
ATOM   3524 C  CD  . PRO B 1 159 ? -11.555 12.984  39.402  1.00 15.95 ? 159 PRO B CD  1 
ATOM   3525 N  N   . GLU B 1 160 ? -10.834 14.551  43.849  1.00 17.83 ? 160 GLU B N   1 
ATOM   3526 C  CA  . GLU B 1 160 ? -9.862  15.305  44.614  1.00 21.30 ? 160 GLU B CA  1 
ATOM   3527 C  C   . GLU B 1 160 ? -8.524  14.561  44.599  1.00 20.67 ? 160 GLU B C   1 
ATOM   3528 O  O   . GLU B 1 160 ? -7.472  15.199  44.657  1.00 21.35 ? 160 GLU B O   1 
ATOM   3529 C  CB  . GLU B 1 160 ? -10.355 15.615  46.042  1.00 25.12 ? 160 GLU B CB  1 
ATOM   3530 C  CG  . GLU B 1 160 ? -11.559 16.533  46.021  1.00 33.71 ? 160 GLU B CG  1 
ATOM   3531 C  CD  . GLU B 1 160 ? -11.915 17.142  47.370  1.00 36.60 ? 160 GLU B CD  1 
ATOM   3532 O  OE1 . GLU B 1 160 ? -12.652 16.477  48.132  1.00 42.31 ? 160 GLU B OE1 1 
ATOM   3533 O  OE2 . GLU B 1 160 ? -11.386 18.244  47.671  1.00 40.42 ? 160 GLU B OE2 1 
ATOM   3534 N  N   . ALA B 1 161 ? -8.555  13.223  44.522  1.00 16.07 ? 161 ALA B N   1 
ATOM   3535 C  CA  . ALA B 1 161 ? -7.330  12.430  44.567  1.00 17.49 ? 161 ALA B CA  1 
ATOM   3536 C  C   . ALA B 1 161 ? -6.536  12.591  43.258  1.00 15.95 ? 161 ALA B C   1 
ATOM   3537 O  O   . ALA B 1 161 ? -5.373  12.173  43.222  1.00 16.50 ? 161 ALA B O   1 
ATOM   3538 C  CB  . ALA B 1 161 ? -7.643  10.985  44.828  1.00 16.65 ? 161 ALA B CB  1 
ATOM   3539 N  N   . LEU B 1 162 ? -7.163  13.136  42.219  1.00 15.75 ? 162 LEU B N   1 
ATOM   3540 C  CA  . LEU B 1 162 ? -6.476  13.421  40.961  1.00 15.43 ? 162 LEU B CA  1 
ATOM   3541 C  C   . LEU B 1 162 ? -5.859  14.809  41.065  1.00 13.86 ? 162 LEU B C   1 
ATOM   3542 O  O   . LEU B 1 162 ? -6.397  15.789  40.510  1.00 17.19 ? 162 LEU B O   1 
ATOM   3543 C  CB  . LEU B 1 162 ? -7.421  13.332  39.766  1.00 14.70 ? 162 LEU B CB  1 
ATOM   3544 C  CG  . LEU B 1 162 ? -6.719  13.528  38.390  1.00 14.54 ? 162 LEU B CG  1 
ATOM   3545 C  CD1 . LEU B 1 162 ? -5.622  12.514  38.203  1.00 14.59 ? 162 LEU B CD1 1 
ATOM   3546 C  CD2 . LEU B 1 162 ? -7.758  13.482  37.299  1.00 14.65 ? 162 LEU B CD2 1 
ATOM   3547 N  N   . ALA B 1 163 ? -4.798  14.879  41.858  1.00 17.89 ? 163 ALA B N   1 
ATOM   3548 C  CA  . ALA B 1 163 ? -4.165  16.143  42.224  1.00 19.53 ? 163 ALA B CA  1 
ATOM   3549 C  C   . ALA B 1 163 ? -3.175  16.516  41.126  1.00 21.53 ? 163 ALA B C   1 
ATOM   3550 O  O   . ALA B 1 163 ? -2.467  15.680  40.581  1.00 22.87 ? 163 ALA B O   1 
ATOM   3551 C  CB  . ALA B 1 163 ? -3.480  15.935  43.568  1.00 20.68 ? 163 ALA B CB  1 
ATOM   3552 N  N   . ASP B 1 164 ? -3.081  17.813  40.838  1.00 21.63 ? 164 ASP B N   1 
ATOM   3553 C  CA  . ASP B 1 164 ? -1.933  18.319  40.095  1.00 20.57 ? 164 ASP B CA  1 
ATOM   3554 C  C   . ASP B 1 164 ? -0.645  18.118  40.893  1.00 18.03 ? 164 ASP B C   1 
ATOM   3555 O  O   . ASP B 1 164 ? -0.622  18.300  42.080  1.00 19.99 ? 164 ASP B O   1 
ATOM   3556 C  CB  . ASP B 1 164 ? -2.099  19.805  39.851  1.00 22.52 ? 164 ASP B CB  1 
ATOM   3557 C  CG  . ASP B 1 164 ? -3.302  20.129  39.002  1.00 27.37 ? 164 ASP B CG  1 
ATOM   3558 O  OD1 . ASP B 1 164 ? -3.468  19.468  38.016  1.00 27.38 ? 164 ASP B OD1 1 
ATOM   3559 O  OD2 . ASP B 1 164 ? -3.995  21.056  39.381  1.00 35.65 ? 164 ASP B OD2 1 
ATOM   3560 N  N   . LEU B 1 165 ? 0.429   17.725  40.224  1.00 16.37 ? 165 LEU B N   1 
ATOM   3561 C  CA  . LEU B 1 165 ? 1.696   17.534  40.898  1.00 17.19 ? 165 LEU B CA  1 
ATOM   3562 C  C   . LEU B 1 165 ? 2.285   18.927  41.121  1.00 20.90 ? 165 LEU B C   1 
ATOM   3563 O  O   . LEU B 1 165 ? 2.241   19.786  40.244  1.00 22.78 ? 165 LEU B O   1 
ATOM   3564 C  CB  . LEU B 1 165 ? 2.639   16.659  40.065  1.00 17.49 ? 165 LEU B CB  1 
ATOM   3565 C  CG  . LEU B 1 165 ? 2.149   15.243  39.833  1.00 16.17 ? 165 LEU B CG  1 
ATOM   3566 C  CD1 . LEU B 1 165 ? 3.144   14.482  38.994  1.00 16.10 ? 165 LEU B CD1 1 
ATOM   3567 C  CD2 . LEU B 1 165 ? 1.923   14.560  41.145  1.00 18.55 ? 165 LEU B CD2 1 
ATOM   3568 N  N   . PRO B 1 166 ? 2.940   19.111  42.263  1.00 19.84 ? 166 PRO B N   1 
ATOM   3569 C  CA  . PRO B 1 166 ? 3.782   20.291  42.443  1.00 23.70 ? 166 PRO B CA  1 
ATOM   3570 C  C   . PRO B 1 166 ? 5.004   20.199  41.546  1.00 22.81 ? 166 PRO B C   1 
ATOM   3571 O  O   . PRO B 1 166 ? 5.288   19.139  41.036  1.00 20.06 ? 166 PRO B O   1 
ATOM   3572 C  CB  . PRO B 1 166 ? 4.115   20.186  43.928  1.00 22.94 ? 166 PRO B CB  1 
ATOM   3573 C  CG  . PRO B 1 166 ? 4.052   18.769  44.295  1.00 25.22 ? 166 PRO B CG  1 
ATOM   3574 C  CD  . PRO B 1 166 ? 3.009   18.155  43.379  1.00 21.38 ? 166 PRO B CD  1 
ATOM   3575 N  N   . LYS B 1 167 ? 5.700   21.333  41.373  1.00 20.66 ? 167 LYS B N   1 
ATOM   3576 C  CA  . LYS B 1 167 ? 6.990   21.408  40.733  1.00 19.75 ? 167 LYS B CA  1 
ATOM   3577 C  C   . LYS B 1 167 ? 7.965   20.790  41.728  1.00 22.93 ? 167 LYS B C   1 
ATOM   3578 O  O   . LYS B 1 167 ? 7.934   21.143  42.905  1.00 28.18 ? 167 LYS B O   1 
ATOM   3579 C  CB  . LYS B 1 167 ? 7.351   22.882  40.484  1.00 27.05 ? 167 LYS B CB  1 
ATOM   3580 N  N   . PHE B 1 168 ? 8.820   19.871  41.282  1.00 18.06 ? 168 PHE B N   1 
ATOM   3581 C  CA  . PHE B 1 168 ? 9.769   19.256  42.195  1.00 15.98 ? 168 PHE B CA  1 
ATOM   3582 C  C   . PHE B 1 168 ? 11.146  19.797  41.841  1.00 15.37 ? 168 PHE B C   1 
ATOM   3583 O  O   . PHE B 1 168 ? 11.420  20.103  40.649  1.00 16.62 ? 168 PHE B O   1 
ATOM   3584 C  CB  . PHE B 1 168 ? 9.770   17.725  42.138  1.00 16.36 ? 168 PHE B CB  1 
ATOM   3585 C  CG  . PHE B 1 168 ? 8.499   17.078  42.622  1.00 18.22 ? 168 PHE B CG  1 
ATOM   3586 C  CD1 . PHE B 1 168 ? 8.220   17.013  43.983  1.00 16.05 ? 168 PHE B CD1 1 
ATOM   3587 C  CD2 . PHE B 1 168 ? 7.540   16.674  41.725  1.00 18.51 ? 168 PHE B CD2 1 
ATOM   3588 C  CE1 . PHE B 1 168 ? 7.041   16.441  44.423  1.00 19.98 ? 168 PHE B CE1 1 
ATOM   3589 C  CE2 . PHE B 1 168 ? 6.376   16.064  42.165  1.00 17.95 ? 168 PHE B CE2 1 
ATOM   3590 C  CZ  . PHE B 1 168 ? 6.130   15.975  43.506  1.00 20.35 ? 168 PHE B CZ  1 
ATOM   3591 N  N   . PRO B 1 169 ? 12.065  19.894  42.829  1.00 17.77 ? 169 PRO B N   1 
ATOM   3592 C  CA  . PRO B 1 169 ? 13.420  20.351  42.532  1.00 19.34 ? 169 PRO B CA  1 
ATOM   3593 C  C   . PRO B 1 169 ? 14.098  19.538  41.442  1.00 19.30 ? 169 PRO B C   1 
ATOM   3594 O  O   . PRO B 1 169 ? 14.007  18.295  41.438  1.00 18.07 ? 169 PRO B O   1 
ATOM   3595 C  CB  . PRO B 1 169 ? 14.208  20.179  43.822  1.00 22.10 ? 169 PRO B CB  1 
ATOM   3596 C  CG  . PRO B 1 169 ? 13.146  20.084  44.896  1.00 24.20 ? 169 PRO B CG  1 
ATOM   3597 C  CD  . PRO B 1 169 ? 11.846  19.601  44.257  1.00 20.14 ? 169 PRO B CD  1 
ATOM   3598 N  N   . GLY B 1 170 ? 14.701  20.254  40.481  1.00 18.33 ? 170 GLY B N   1 
ATOM   3599 C  CA  . GLY B 1 170 ? 15.385  19.652  39.346  1.00 19.73 ? 170 GLY B CA  1 
ATOM   3600 C  C   . GLY B 1 170 ? 14.488  19.148  38.187  1.00 18.67 ? 170 GLY B C   1 
ATOM   3601 O  O   . GLY B 1 170 ? 15.012  18.635  37.243  1.00 20.66 ? 170 GLY B O   1 
ATOM   3602 N  N   . ASP B 1 171 ? 13.169  19.288  38.294  1.00 16.34 ? 171 ASP B N   1 
ATOM   3603 C  CA  . ASP B 1 171 ? 12.263  19.011  37.171  1.00 18.82 ? 171 ASP B CA  1 
ATOM   3604 C  C   . ASP B 1 171 ? 12.708  19.824  35.955  1.00 19.33 ? 171 ASP B C   1 
ATOM   3605 O  O   . ASP B 1 171 ? 13.039  21.022  36.017  1.00 21.62 ? 171 ASP B O   1 
ATOM   3606 C  CB  . ASP B 1 171 ? 10.825  19.495  37.406  1.00 19.20 ? 171 ASP B CB  1 
ATOM   3607 C  CG  . ASP B 1 171 ? 9.873   18.640  38.225  1.00 21.37 ? 171 ASP B CG  1 
ATOM   3608 O  OD1 . ASP B 1 171 ? 10.232  17.478  38.493  1.00 21.03 ? 171 ASP B OD1 1 
ATOM   3609 O  OD2 . ASP B 1 171 ? 8.707   19.223  38.490  1.00 24.68 ? 171 ASP B OD2 1 
ATOM   3610 N  N   . ASN B 1 172 ? 12.646  19.188  34.811  1.00 18.26 ? 172 ASN B N   1 
ATOM   3611 C  CA  . ASN B 1 172 ? 12.861  19.829  33.533  1.00 18.42 ? 172 ASN B CA  1 
ATOM   3612 C  C   . ASN B 1 172 ? 11.859  19.249  32.544  1.00 16.06 ? 172 ASN B C   1 
ATOM   3613 O  O   . ASN B 1 172 ? 12.221  18.537  31.624  1.00 17.77 ? 172 ASN B O   1 
ATOM   3614 C  CB  . ASN B 1 172 ? 14.294  19.611  33.086  1.00 23.72 ? 172 ASN B CB  1 
ATOM   3615 C  CG  . ASN B 1 172 ? 14.664  20.396  31.869  1.00 27.35 ? 172 ASN B CG  1 
ATOM   3616 O  OD1 . ASN B 1 172 ? 13.960  21.327  31.547  1.00 26.98 ? 172 ASN B OD1 1 
ATOM   3617 N  ND2 . ASN B 1 172 ? 15.694  19.932  31.172  1.00 35.35 ? 172 ASN B ND2 1 
ATOM   3618 N  N   . LEU B 1 173 ? 10.603  19.632  32.719  1.00 17.72 ? 173 LEU B N   1 
ATOM   3619 C  CA  . LEU B 1 173 ? 9.553   18.889  32.050  1.00 19.34 ? 173 LEU B CA  1 
ATOM   3620 C  C   . LEU B 1 173 ? 9.360   19.443  30.640  1.00 19.44 ? 173 LEU B C   1 
ATOM   3621 O  O   . LEU B 1 173 ? 9.292   20.653  30.473  1.00 20.40 ? 173 LEU B O   1 
ATOM   3622 C  CB  . LEU B 1 173 ? 8.280   19.042  32.871  1.00 18.23 ? 173 LEU B CB  1 
ATOM   3623 C  CG  . LEU B 1 173 ? 8.339   18.425  34.268  1.00 17.67 ? 173 LEU B CG  1 
ATOM   3624 C  CD1 . LEU B 1 173 ? 6.930   18.531  34.888  1.00 21.47 ? 173 LEU B CD1 1 
ATOM   3625 C  CD2 . LEU B 1 173 ? 8.849   17.005  34.279  1.00 17.92 ? 173 LEU B CD2 1 
ATOM   3626 N  N   . ASP B 1 174 ? 9.359   18.563  29.641  1.00 16.38 ? 174 ASP B N   1 
ATOM   3627 C  CA  . ASP B 1 174 ? 9.023   18.950  28.282  1.00 17.82 ? 174 ASP B CA  1 
ATOM   3628 C  C   . ASP B 1 174 ? 7.512   18.967  28.177  1.00 21.44 ? 174 ASP B C   1 
ATOM   3629 O  O   . ASP B 1 174 ? 6.878   17.900  28.278  1.00 18.57 ? 174 ASP B O   1 
ATOM   3630 C  CB  . ASP B 1 174 ? 9.713   17.994  27.332  1.00 20.11 ? 174 ASP B CB  1 
ATOM   3631 C  CG  . ASP B 1 174 ? 9.438   18.202  25.850  1.00 24.48 ? 174 ASP B CG  1 
ATOM   3632 O  OD1 . ASP B 1 174 ? 8.552   18.983  25.518  1.00 24.74 ? 174 ASP B OD1 1 
ATOM   3633 O  OD2 . ASP B 1 174 ? 10.123  17.584  25.095  1.00 27.96 ? 174 ASP B OD2 1 
ATOM   3634 N  N   . ARG B 1 175 ? 6.939   20.165  27.929  1.00 21.11 ? 175 ARG B N   1 
ATOM   3635 C  CA  . ARG B 1 175 ? 5.484   20.319  27.848  1.00 24.53 ? 175 ARG B CA  1 
ATOM   3636 C  C   . ARG B 1 175 ? 4.896   19.415  26.746  1.00 24.08 ? 175 ARG B C   1 
ATOM   3637 O  O   . ARG B 1 175 ? 3.781   18.942  26.904  1.00 23.45 ? 175 ARG B O   1 
ATOM   3638 C  CB  . ARG B 1 175 ? 5.117   21.796  27.623  1.00 31.76 ? 175 ARG B CB  1 
ATOM   3639 C  CG  . ARG B 1 175 ? 5.124   22.664  28.880  1.00 37.54 ? 175 ARG B CG  1 
ATOM   3640 N  N   . ALA B 1 176 ? 5.652   19.063  25.703  1.00 20.62 ? 176 ALA B N   1 
ATOM   3641 C  CA  . ALA B 1 176 ? 5.141   18.294  24.566  1.00 23.62 ? 176 ALA B CA  1 
ATOM   3642 C  C   . ALA B 1 176 ? 5.037   16.818  24.940  1.00 23.66 ? 176 ALA B C   1 
ATOM   3643 O  O   . ALA B 1 176 ? 4.294   16.087  24.318  1.00 26.15 ? 176 ALA B O   1 
ATOM   3644 C  CB  . ALA B 1 176 ? 6.005   18.470  23.346  1.00 25.13 ? 176 ALA B CB  1 
ATOM   3645 N  N   . ARG B 1 177 ? 5.814   16.383  25.936  1.00 17.81 ? 177 ARG B N   1 
ATOM   3646 C  CA  . ARG B 1 177 ? 5.809   15.022  26.389  1.00 22.12 ? 177 ARG B CA  1 
ATOM   3647 C  C   . ARG B 1 177 ? 5.259   14.912  27.808  1.00 17.05 ? 177 ARG B C   1 
ATOM   3648 O  O   . ARG B 1 177 ? 5.635   13.997  28.535  1.00 17.83 ? 177 ARG B O   1 
ATOM   3649 C  CB  . ARG B 1 177 ? 7.239   14.462  26.318  1.00 26.73 ? 177 ARG B CB  1 
ATOM   3650 C  CG  . ARG B 1 177 ? 7.652   14.116  24.895  1.00 34.11 ? 177 ARG B CG  1 
ATOM   3651 C  CD  . ARG B 1 177 ? 9.099   13.662  24.902  1.00 36.89 ? 177 ARG B CD  1 
ATOM   3652 N  NE  . ARG B 1 177 ? 9.270   12.551  23.982  1.00 41.11 ? 177 ARG B NE  1 
ATOM   3653 C  CZ  . ARG B 1 177 ? 10.439  12.034  23.627  1.00 48.52 ? 177 ARG B CZ  1 
ATOM   3654 N  NH1 . ARG B 1 177 ? 11.555  12.753  23.693  1.00 50.15 ? 177 ARG B NH1 1 
ATOM   3655 N  NH2 . ARG B 1 177 ? 10.463  10.802  23.154  1.00 58.44 ? 177 ARG B NH2 1 
ATOM   3656 N  N   . SER B 1 178 ? 4.366   15.821  28.150  1.00 13.66 ? 178 SER B N   1 
ATOM   3657 C  CA  . SER B 1 178 ? 3.675   15.913  29.419  1.00 14.68 ? 178 SER B CA  1 
ATOM   3658 C  C   . SER B 1 178 ? 2.169   16.082  29.171  1.00 14.09 ? 178 SER B C   1 
ATOM   3659 O  O   . SER B 1 178 ? 1.753   16.542  28.100  1.00 16.08 ? 178 SER B O   1 
ATOM   3660 C  CB  . SER B 1 178 ? 4.232   17.050  30.232  1.00 15.29 ? 178 SER B CB  1 
ATOM   3661 O  OG  . SER B 1 178 ? 5.602   16.847  30.535  1.00 14.18 ? 178 SER B OG  1 
ATOM   3662 N  N   . GLY B 1 179 ? 1.409   15.778  30.218  1.00 15.44 ? 179 GLY B N   1 
ATOM   3663 C  CA  . GLY B 1 179 ? -0.023  15.913  30.260  1.00 13.85 ? 179 GLY B CA  1 
ATOM   3664 C  C   . GLY B 1 179 ? -0.747  15.017  29.273  1.00 12.93 ? 179 GLY B C   1 
ATOM   3665 O  O   . GLY B 1 179 ? -0.255  13.968  28.893  1.00 14.65 ? 179 GLY B O   1 
ATOM   3666 N  N   . GLY B 1 180 ? -1.931  15.453  28.882  1.00 13.69 ? 180 GLY B N   1 
ATOM   3667 C  CA  . GLY B 1 180 ? -2.789  14.651  28.057  1.00 12.83 ? 180 GLY B CA  1 
ATOM   3668 C  C   . GLY B 1 180 ? -4.155  14.500  28.689  1.00 12.03 ? 180 GLY B C   1 
ATOM   3669 O  O   . GLY B 1 180 ? -4.280  14.208  29.875  1.00 14.10 ? 180 GLY B O   1 
ATOM   3670 N  N   . ASP B 1 181 ? -5.150  14.555  27.832  1.00 12.14 ? 181 ASP B N   1 
ATOM   3671 C  CA  . ASP B 1 181 ? -6.533  14.380  28.244  1.00 11.87 ? 181 ASP B CA  1 
ATOM   3672 C  C   . ASP B 1 181 ? -6.814  12.937  28.610  1.00 13.72 ? 181 ASP B C   1 
ATOM   3673 O  O   . ASP B 1 181 ? -7.635  12.723  29.515  1.00 11.54 ? 181 ASP B O   1 
ATOM   3674 C  CB  . ASP B 1 181 ? -7.529  14.770  27.149  1.00 12.59 ? 181 ASP B CB  1 
ATOM   3675 C  CG  . ASP B 1 181 ? -7.544  16.266  26.853  1.00 15.97 ? 181 ASP B CG  1 
ATOM   3676 O  OD1 . ASP B 1 181 ? -7.173  17.050  27.761  1.00 15.84 ? 181 ASP B OD1 1 
ATOM   3677 O  OD2 . ASP B 1 181 ? -7.801  16.609  25.671  1.00 18.75 ? 181 ASP B OD2 1 
ATOM   3678 N  N   . LEU B 1 182 ? -6.197  11.984  27.880  1.00 14.38 ? 182 LEU B N   1 
ATOM   3679 C  CA  . LEU B 1 182 ? -6.350  10.602  28.319  1.00 15.54 ? 182 LEU B CA  1 
ATOM   3680 C  C   . LEU B 1 182 ? -5.146  9.767   27.929  1.00 12.97 ? 182 LEU B C   1 
ATOM   3681 O  O   . LEU B 1 182 ? -4.310  10.247  27.194  1.00 13.16 ? 182 LEU B O   1 
ATOM   3682 C  CB  . LEU B 1 182 ? -7.616  10.009  27.749  1.00 21.83 ? 182 LEU B CB  1 
ATOM   3683 C  CG  . LEU B 1 182 ? -7.718  9.895   26.260  1.00 23.52 ? 182 LEU B CG  1 
ATOM   3684 C  CD1 . LEU B 1 182 ? -7.399  8.471   25.875  1.00 28.55 ? 182 LEU B CD1 1 
ATOM   3685 C  CD2 . LEU B 1 182 ? -9.116  10.174  25.804  1.00 30.75 ? 182 LEU B CD2 1 
ATOM   3686 N  N   . CYS B 1 183 ? -5.068  8.544   28.469  1.00 10.97 ? 183 CYS B N   1 
ATOM   3687 C  CA  . CYS B 1 183 ? -3.923  7.705   28.189  1.00 10.86 ? 183 CYS B CA  1 
ATOM   3688 C  C   . CYS B 1 183 ? -4.496  6.302   27.896  1.00 10.97 ? 183 CYS B C   1 
ATOM   3689 O  O   . CYS B 1 183 ? -5.574  5.927   28.355  1.00 10.69 ? 183 CYS B O   1 
ATOM   3690 C  CB  . CYS B 1 183 ? -2.866  7.647   29.306  1.00 12.57 ? 183 CYS B CB  1 
ATOM   3691 S  SG  . CYS B 1 183 ? -3.465  6.806   30.778  1.00 15.53 ? 183 CYS B SG  1 
ATOM   3692 N  N   . VAL B 1 184 ? -3.743  5.587   27.089  1.00 11.28 ? 184 VAL B N   1 
ATOM   3693 C  CA  . VAL B 1 184 ? -3.891  4.161   26.985  1.00 10.86 ? 184 VAL B CA  1 
ATOM   3694 C  C   . VAL B 1 184 ? -2.534  3.551   27.248  1.00 12.02 ? 184 VAL B C   1 
ATOM   3695 O  O   . VAL B 1 184 ? -1.583  3.816   26.512  1.00 11.60 ? 184 VAL B O   1 
ATOM   3696 C  CB  . VAL B 1 184 ? -4.408  3.740   25.599  1.00 12.94 ? 184 VAL B CB  1 
ATOM   3697 C  CG1 . VAL B 1 184 ? -4.573  2.201   25.595  1.00 14.71 ? 184 VAL B CG1 1 
ATOM   3698 C  CG2 . VAL B 1 184 ? -5.703  4.456   25.311  1.00 14.87 ? 184 VAL B CG2 1 
ATOM   3699 N  N   . GLN B 1 185 ? -2.520  2.641   28.210  1.00 10.24 ? 185 GLN B N   1 
ATOM   3700 C  CA  . GLN B 1 185 ? -1.332  1.872   28.515  1.00 10.46 ? 185 GLN B CA  1 
ATOM   3701 C  C   . GLN B 1 185 ? -1.484  0.499   27.845  1.00 9.93  ? 185 GLN B C   1 
ATOM   3702 O  O   . GLN B 1 185 ? -2.424  -0.205  28.161  1.00 10.13 ? 185 GLN B O   1 
ATOM   3703 C  CB  . GLN B 1 185 ? -1.236  1.664   30.039  1.00 10.57 ? 185 GLN B CB  1 
ATOM   3704 C  CG  . GLN B 1 185 ? -0.016  0.824   30.457  1.00 11.13 ? 185 GLN B CG  1 
ATOM   3705 C  CD  . GLN B 1 185 ? -0.068  0.404   31.912  1.00 13.44 ? 185 GLN B CD  1 
ATOM   3706 O  OE1 . GLN B 1 185 ? 0.434   1.095   32.792  1.00 15.66 ? 185 GLN B OE1 1 
ATOM   3707 N  NE2 . GLN B 1 185 ? -0.763  -0.686  32.191  1.00 13.94 ? 185 GLN B NE2 1 
ATOM   3708 N  N   . ALA B 1 186 ? -0.658  0.156   26.902  1.00 9.04  ? 186 ALA B N   1 
ATOM   3709 C  CA  . ALA B 1 186 ? -0.731  -1.118  26.214  1.00 9.72  ? 186 ALA B CA  1 
ATOM   3710 C  C   . ALA B 1 186 ? 0.506   -1.915  26.603  1.00 10.93 ? 186 ALA B C   1 
ATOM   3711 O  O   . ALA B 1 186 ? 1.653   -1.465  26.375  1.00 13.02 ? 186 ALA B O   1 
ATOM   3712 C  CB  . ALA B 1 186 ? -0.792  -0.906  24.703  1.00 10.20 ? 186 ALA B CB  1 
ATOM   3713 N  N   . CYS B 1 187 ? 0.294   -3.032  27.335  1.00 11.39 ? 187 CYS B N   1 
ATOM   3714 C  CA  . CYS B 1 187 ? 1.384   -3.885  27.752  1.00 11.54 ? 187 CYS B CA  1 
ATOM   3715 C  C   . CYS B 1 187 ? 1.169   -5.241  27.140  1.00 12.66 ? 187 CYS B C   1 
ATOM   3716 O  O   . CYS B 1 187 ? 0.052   -5.733  27.117  1.00 12.66 ? 187 CYS B O   1 
ATOM   3717 C  CB  . CYS B 1 187 ? 1.410   -4.073  29.258  1.00 13.01 ? 187 CYS B CB  1 
ATOM   3718 S  SG  . CYS B 1 187 ? 1.749   -2.511  30.152  1.00 13.12 ? 187 CYS B SG  1 
ATOM   3719 N  N   . ALA B 1 188 ? 2.254   -5.827  26.602  1.00 12.54 ? 188 ALA B N   1 
ATOM   3720 C  CA  . ALA B 1 188 ? 2.139   -7.123  25.984  1.00 11.31 ? 188 ALA B CA  1 
ATOM   3721 C  C   . ALA B 1 188 ? 3.553   -7.682  25.933  1.00 13.12 ? 188 ALA B C   1 
ATOM   3722 O  O   . ALA B 1 188 ? 4.545   -6.976  26.169  1.00 9.98  ? 188 ALA B O   1 
ATOM   3723 C  CB  . ALA B 1 188 ? 1.567   -6.995  24.649  1.00 10.42 ? 188 ALA B CB  1 
ATOM   3724 N  N   . ASP B 1 189 ? 3.680   -8.980  25.692  1.00 11.53 ? 189 ASP B N   1 
ATOM   3725 C  CA  . ASP B 1 189 ? 5.022   -9.545  25.634  1.00 13.60 ? 189 ASP B CA  1 
ATOM   3726 C  C   . ASP B 1 189 ? 5.652   -9.298  24.279  1.00 13.96 ? 189 ASP B C   1 
ATOM   3727 O  O   . ASP B 1 189 ? 6.848   -9.402  24.167  1.00 17.31 ? 189 ASP B O   1 
ATOM   3728 C  CB  . ASP B 1 189 ? 5.035   -11.061 25.916  1.00 14.28 ? 189 ASP B CB  1 
ATOM   3729 C  CG  . ASP B 1 189 ? 4.613   -11.309 27.360  1.00 15.35 ? 189 ASP B CG  1 
ATOM   3730 O  OD1 . ASP B 1 189 ? 4.975   -10.487 28.223  1.00 15.20 ? 189 ASP B OD1 1 
ATOM   3731 O  OD2 . ASP B 1 189 ? 3.935   -12.321 27.605  1.00 15.78 ? 189 ASP B OD2 1 
ATOM   3732 N  N   . ASP B 1 190 ? 4.868   -8.972  23.291  1.00 12.86 ? 190 ASP B N   1 
ATOM   3733 C  CA  . ASP B 1 190 ? 5.371   -8.775  21.931  1.00 13.78 ? 190 ASP B CA  1 
ATOM   3734 C  C   . ASP B 1 190 ? 5.127   -7.306  21.604  1.00 11.50 ? 190 ASP B C   1 
ATOM   3735 O  O   . ASP B 1 190 ? 3.998   -6.823  21.668  1.00 12.37 ? 190 ASP B O   1 
ATOM   3736 C  CB  . ASP B 1 190 ? 4.587   -9.655  20.975  1.00 13.74 ? 190 ASP B CB  1 
ATOM   3737 C  CG  . ASP B 1 190 ? 5.034   -9.559  19.519  1.00 17.26 ? 190 ASP B CG  1 
ATOM   3738 O  OD1 . ASP B 1 190 ? 5.419   -8.424  19.059  1.00 16.98 ? 190 ASP B OD1 1 
ATOM   3739 O  OD2 . ASP B 1 190 ? 4.743   -10.534 18.834  1.00 19.46 ? 190 ASP B OD2 1 
ATOM   3740 N  N   . PRO B 1 191 ? 6.174   -6.500  21.350  1.00 12.29 ? 191 PRO B N   1 
ATOM   3741 C  CA  . PRO B 1 191 ? 5.932   -5.060  21.165  1.00 12.13 ? 191 PRO B CA  1 
ATOM   3742 C  C   . PRO B 1 191 ? 5.078   -4.727  19.937  1.00 12.87 ? 191 PRO B C   1 
ATOM   3743 O  O   . PRO B 1 191 ? 4.413   -3.703  19.931  1.00 12.92 ? 191 PRO B O   1 
ATOM   3744 C  CB  . PRO B 1 191 ? 7.319   -4.474  21.007  1.00 12.68 ? 191 PRO B CB  1 
ATOM   3745 C  CG  . PRO B 1 191 ? 8.173   -5.629  20.560  1.00 14.86 ? 191 PRO B CG  1 
ATOM   3746 C  CD  . PRO B 1 191 ? 7.593   -6.897  21.143  1.00 14.42 ? 191 PRO B CD  1 
ATOM   3747 N  N   . GLN B 1 192 ? 5.062   -5.603  18.909  1.00 12.00 ? 192 GLN B N   1 
ATOM   3748 C  CA  . GLN B 1 192 ? 4.234   -5.344  17.752  1.00 13.71 ? 192 GLN B CA  1 
ATOM   3749 C  C   . GLN B 1 192 ? 2.772   -5.501  18.098  1.00 12.45 ? 192 GLN B C   1 
ATOM   3750 O  O   . GLN B 1 192 ? 1.943   -4.788  17.555  1.00 14.64 ? 192 GLN B O   1 
ATOM   3751 C  CB  . GLN B 1 192 ? 4.697   -6.188  16.555  1.00 16.09 ? 192 GLN B CB  1 
ATOM   3752 C  CG  . GLN B 1 192 ? 3.909   -5.838  15.279  1.00 15.82 ? 192 GLN B CG  1 
ATOM   3753 C  CD  . GLN B 1 192 ? 4.799   -6.011  14.072  1.00 20.23 ? 192 GLN B CD  1 
ATOM   3754 O  OE1 . GLN B 1 192 ? 6.021   -5.788  14.171  1.00 18.90 ? 192 GLN B OE1 1 
ATOM   3755 N  NE2 . GLN B 1 192 ? 4.237   -6.537  12.973  1.00 14.95 ? 192 GLN B NE2 1 
ATOM   3756 N  N   . VAL B 1 193 ? 2.420   -6.373  19.054  1.00 11.66 ? 193 VAL B N   1 
ATOM   3757 C  CA  . VAL B 1 193 ? 1.033   -6.455  19.525  1.00 11.06 ? 193 VAL B CA  1 
ATOM   3758 C  C   . VAL B 1 193 ? 0.598   -5.167  20.217  1.00 11.47 ? 193 VAL B C   1 
ATOM   3759 O  O   . VAL B 1 193 ? -0.489  -4.639  19.965  1.00 10.92 ? 193 VAL B O   1 
ATOM   3760 C  CB  . VAL B 1 193 ? 0.851   -7.718  20.397  1.00 11.71 ? 193 VAL B CB  1 
ATOM   3761 C  CG1 . VAL B 1 193 ? -0.526  -7.754  21.060  1.00 11.94 ? 193 VAL B CG1 1 
ATOM   3762 C  CG2 . VAL B 1 193 ? 1.127   -8.946  19.519  1.00 13.03 ? 193 VAL B CG2 1 
ATOM   3763 N  N   . ALA B 1 194 ? 1.497   -4.608  21.044  1.00 12.16 ? 194 ALA B N   1 
ATOM   3764 C  CA  . ALA B 1 194 ? 1.248   -3.361  21.757  1.00 11.58 ? 194 ALA B CA  1 
ATOM   3765 C  C   . ALA B 1 194 ? 1.089   -2.202  20.746  1.00 11.04 ? 194 ALA B C   1 
ATOM   3766 O  O   . ALA B 1 194 ? 0.148   -1.402  20.838  1.00 12.70 ? 194 ALA B O   1 
ATOM   3767 C  CB  . ALA B 1 194 ? 2.324   -3.028  22.795  1.00 12.13 ? 194 ALA B CB  1 
ATOM   3768 N  N   . VAL B 1 195 ? 2.040   -2.063  19.817  1.00 12.69 ? 195 VAL B N   1 
ATOM   3769 C  CA  . VAL B 1 195 ? 1.992   -0.972  18.846  1.00 12.24 ? 195 VAL B CA  1 
ATOM   3770 C  C   . VAL B 1 195 ? 0.734   -1.049  17.990  1.00 12.58 ? 195 VAL B C   1 
ATOM   3771 O  O   . VAL B 1 195 ? 0.081   -0.038  17.739  1.00 11.40 ? 195 VAL B O   1 
ATOM   3772 C  CB  . VAL B 1 195 ? 3.259   -0.953  17.967  1.00 14.93 ? 195 VAL B CB  1 
ATOM   3773 C  CG1 . VAL B 1 195 ? 3.067   -0.047  16.762  1.00 16.02 ? 195 VAL B CG1 1 
ATOM   3774 C  CG2 . VAL B 1 195 ? 4.460   -0.603  18.809  1.00 16.37 ? 195 VAL B CG2 1 
ATOM   3775 N  N   . HIS B 1 196 ? 0.392   -2.261  17.558  1.00 10.80 ? 196 HIS B N   1 
ATOM   3776 C  CA  . HIS B 1 196 ? -0.783  -2.477  16.742  1.00 11.15 ? 196 HIS B CA  1 
ATOM   3777 C  C   . HIS B 1 196 ? -2.054  -1.975  17.427  1.00 9.96  ? 196 HIS B C   1 
ATOM   3778 O  O   . HIS B 1 196 ? -2.921  -1.311  16.832  1.00 11.19 ? 196 HIS B O   1 
ATOM   3779 C  CB  . HIS B 1 196 ? -0.886  -3.938  16.349  1.00 11.43 ? 196 HIS B CB  1 
ATOM   3780 C  CG  . HIS B 1 196 ? -2.213  -4.308  15.740  1.00 11.41 ? 196 HIS B CG  1 
ATOM   3781 N  ND1 . HIS B 1 196 ? -3.239  -4.888  16.487  1.00 12.50 ? 196 HIS B ND1 1 
ATOM   3782 C  CD2 . HIS B 1 196 ? -2.651  -4.199  14.445  1.00 10.78 ? 196 HIS B CD2 1 
ATOM   3783 C  CE1 . HIS B 1 196 ? -4.282  -5.044  15.680  1.00 11.36 ? 196 HIS B CE1 1 
ATOM   3784 N  NE2 . HIS B 1 196 ? -3.912  -4.689  14.392  1.00 12.04 ? 196 HIS B NE2 1 
ATOM   3785 N  N   . ALA B 1 197 ? -2.146  -2.243  18.740  1.00 11.45 ? 197 ALA B N   1 
ATOM   3786 C  CA  . ALA B 1 197 ? -3.238  -1.795  19.554  1.00 10.66 ? 197 ALA B CA  1 
ATOM   3787 C  C   . ALA B 1 197 ? -3.318  -0.293  19.510  1.00 10.52 ? 197 ALA B C   1 
ATOM   3788 O  O   . ALA B 1 197 ? -4.394  0.244   19.235  1.00 11.74 ? 197 ALA B O   1 
ATOM   3789 C  CB  . ALA B 1 197 ? -3.082  -2.326  20.987  1.00 11.00 ? 197 ALA B CB  1 
ATOM   3790 N  N   . ILE B 1 198 ? -2.200  0.377   19.802  1.00 11.22 ? 198 ILE B N   1 
ATOM   3791 C  CA  . ILE B 1 198 ? -2.208  1.832   19.874  1.00 11.75 ? 198 ILE B CA  1 
ATOM   3792 C  C   . ILE B 1 198 ? -2.535  2.428   18.527  1.00 11.15 ? 198 ILE B C   1 
ATOM   3793 O  O   . ILE B 1 198 ? -3.417  3.324   18.445  1.00 11.77 ? 198 ILE B O   1 
ATOM   3794 C  CB  . ILE B 1 198 ? -0.903  2.391   20.481  1.00 12.19 ? 198 ILE B CB  1 
ATOM   3795 C  CG1 . ILE B 1 198 ? -0.708  1.912   21.927  1.00 14.53 ? 198 ILE B CG1 1 
ATOM   3796 C  CG2 . ILE B 1 198 ? -0.919  3.911   20.372  1.00 12.84 ? 198 ILE B CG2 1 
ATOM   3797 C  CD1 . ILE B 1 198 ? -1.762  2.334   22.915  1.00 15.88 ? 198 ILE B CD1 1 
ATOM   3798 N  N   . ARG B 1 199 ? -1.911  1.883   17.467  1.00 11.34 ? 199 ARG B N   1 
ATOM   3799 C  CA  . ARG B 1 199 ? -2.100  2.384   16.121  1.00 11.56 ? 199 ARG B CA  1 
ATOM   3800 C  C   . ARG B 1 199 ? -3.557  2.327   15.712  1.00 12.08 ? 199 ARG B C   1 
ATOM   3801 O  O   . ARG B 1 199 ? -4.085  3.255   15.098  1.00 11.05 ? 199 ARG B O   1 
ATOM   3802 C  CB  . ARG B 1 199 ? -1.179  1.625   15.172  1.00 12.11 ? 199 ARG B CB  1 
ATOM   3803 C  CG  . ARG B 1 199 ? -1.034  2.244   13.766  1.00 13.89 ? 199 ARG B CG  1 
ATOM   3804 C  CD  . ARG B 1 199 ? -1.980  1.533   12.881  1.00 13.53 ? 199 ARG B CD  1 
ATOM   3805 N  NE  . ARG B 1 199 ? -1.593  1.784   11.470  1.00 13.49 ? 199 ARG B NE  1 
ATOM   3806 C  CZ  . ARG B 1 199 ? -0.698  1.083   10.786  1.00 13.83 ? 199 ARG B CZ  1 
ATOM   3807 N  NH1 . ARG B 1 199 ? 0.094   0.203   11.412  1.00 14.40 ? 199 ARG B NH1 1 
ATOM   3808 N  NH2 . ARG B 1 199 ? -0.617  1.279   9.461   1.00 12.73 ? 199 ARG B NH2 1 
ATOM   3809 N  N   . ASN B 1 200 ? -4.206  1.193   16.029  1.00 11.90 ? 200 ASN B N   1 
ATOM   3810 C  CA  . ASN B 1 200 ? -5.585  1.002   15.661  1.00 10.75 ? 200 ASN B CA  1 
ATOM   3811 C  C   . ASN B 1 200 ? -6.536  1.792   16.522  1.00 10.73 ? 200 ASN B C   1 
ATOM   3812 O  O   . ASN B 1 200 ? -7.491  2.318   15.964  1.00 12.28 ? 200 ASN B O   1 
ATOM   3813 C  CB  . ASN B 1 200 ? -5.961  -0.481  15.603  1.00 10.10 ? 200 ASN B CB  1 
ATOM   3814 C  CG  . ASN B 1 200 ? -5.457  -1.147  14.350  1.00 11.42 ? 200 ASN B CG  1 
ATOM   3815 O  OD1 . ASN B 1 200 ? -6.190  -1.204  13.356  1.00 13.56 ? 200 ASN B OD1 1 
ATOM   3816 N  ND2 . ASN B 1 200 ? -4.171  -1.474  14.331  1.00 11.56 ? 200 ASN B ND2 1 
ATOM   3817 N  N   . LEU B 1 201 ? -6.332  1.916   17.838  1.00 9.73  ? 201 LEU B N   1 
ATOM   3818 C  CA  . LEU B 1 201 ? -7.186  2.838   18.635  1.00 11.87 ? 201 LEU B CA  1 
ATOM   3819 C  C   . LEU B 1 201 ? -7.056  4.260   18.096  1.00 11.67 ? 201 LEU B C   1 
ATOM   3820 O  O   . LEU B 1 201 ? -8.012  4.966   18.021  1.00 13.04 ? 201 LEU B O   1 
ATOM   3821 C  CB  . LEU B 1 201 ? -6.775  2.758   20.111  1.00 12.62 ? 201 LEU B CB  1 
ATOM   3822 C  CG  . LEU B 1 201 ? -7.123  1.454   20.833  1.00 16.17 ? 201 LEU B CG  1 
ATOM   3823 C  CD1 . LEU B 1 201 ? -6.629  1.534   22.273  1.00 19.70 ? 201 LEU B CD1 1 
ATOM   3824 C  CD2 . LEU B 1 201 ? -8.611  1.125   20.811  1.00 19.42 ? 201 LEU B CD2 1 
ATOM   3825 N  N   . ALA B 1 202 ? -5.851  4.723   17.795  1.00 12.50 ? 202 ALA B N   1 
ATOM   3826 C  CA  . ALA B 1 202 ? -5.640  6.067   17.278  1.00 14.86 ? 202 ALA B CA  1 
ATOM   3827 C  C   . ALA B 1 202 ? -6.398  6.267   15.971  1.00 13.86 ? 202 ALA B C   1 
ATOM   3828 O  O   . ALA B 1 202 ? -7.046  7.281   15.798  1.00 15.41 ? 202 ALA B O   1 
ATOM   3829 C  CB  . ALA B 1 202 ? -4.150  6.398   17.105  1.00 12.79 ? 202 ALA B CB  1 
ATOM   3830 N  N   . ARG B 1 203 ? -6.359  5.255   15.111  1.00 13.45 ? 203 ARG B N   1 
ATOM   3831 C  CA  . ARG B 1 203 ? -7.080  5.305   13.849  1.00 14.84 ? 203 ARG B CA  1 
ATOM   3832 C  C   . ARG B 1 203 ? -8.589  5.388   14.037  1.00 14.17 ? 203 ARG B C   1 
ATOM   3833 O  O   . ARG B 1 203 ? -9.285  6.202   13.390  1.00 13.88 ? 203 ARG B O   1 
ATOM   3834 C  CB  . ARG B 1 203 ? -6.642  4.118   13.001  1.00 14.45 ? 203 ARG B CB  1 
ATOM   3835 C  CG  . ARG B 1 203 ? -7.429  4.004   11.705  1.00 19.18 ? 203 ARG B CG  1 
ATOM   3836 C  CD  . ARG B 1 203 ? -6.721  3.137   10.715  1.00 20.34 ? 203 ARG B CD  1 
ATOM   3837 N  NE  . ARG B 1 203 ? -7.544  3.108   9.511   1.00 22.89 ? 203 ARG B NE  1 
ATOM   3838 C  CZ  . ARG B 1 203 ? -8.265  2.068   9.120   1.00 27.26 ? 203 ARG B CZ  1 
ATOM   3839 N  NH1 . ARG B 1 203 ? -8.550  1.082   9.948   1.00 24.17 ? 203 ARG B NH1 1 
ATOM   3840 N  NH2 . ARG B 1 203 ? -8.752  2.063   7.898   1.00 30.77 ? 203 ARG B NH2 1 
ATOM   3841 N  N   . ILE B 1 204 ? -9.118  4.504   14.903  1.00 14.03 ? 204 ILE B N   1 
ATOM   3842 C  CA  . ILE B 1 204 ? -10.541 4.522   15.228  1.00 14.80 ? 204 ILE B CA  1 
ATOM   3843 C  C   . ILE B 1 204 ? -10.939 5.927   15.702  1.00 18.50 ? 204 ILE B C   1 
ATOM   3844 O  O   . ILE B 1 204 ? -12.034 6.412   15.375  1.00 15.97 ? 204 ILE B O   1 
ATOM   3845 C  CB  . ILE B 1 204 ? -10.910 3.402   16.235  1.00 15.04 ? 204 ILE B CB  1 
ATOM   3846 C  CG1 . ILE B 1 204 ? -10.815 2.038   15.572  1.00 17.20 ? 204 ILE B CG1 1 
ATOM   3847 C  CG2 . ILE B 1 204 ? -12.309 3.602   16.810  1.00 17.09 ? 204 ILE B CG2 1 
ATOM   3848 C  CD1 . ILE B 1 204 ? -10.795 0.891   16.593  1.00 19.27 ? 204 ILE B CD1 1 
ATOM   3849 N  N   . GLY B 1 205 ? -10.093 6.538   16.516  1.00 14.34 ? 205 GLY B N   1 
ATOM   3850 C  CA  . GLY B 1 205 ? -10.445 7.825   17.099  1.00 15.27 ? 205 GLY B CA  1 
ATOM   3851 C  C   . GLY B 1 205 ? -10.159 9.060   16.244  1.00 17.14 ? 205 GLY B C   1 
ATOM   3852 O  O   . GLY B 1 205 ? -10.363 10.165  16.724  1.00 17.46 ? 205 GLY B O   1 
ATOM   3853 N  N   . PHE B 1 206 ? -9.652  8.872   15.028  1.00 19.25 ? 206 PHE B N   1 
ATOM   3854 C  CA  . PHE B 1 206 ? -9.155  9.985   14.232  1.00 23.27 ? 206 PHE B CA  1 
ATOM   3855 C  C   . PHE B 1 206 ? -10.340 10.905  13.966  1.00 21.10 ? 206 PHE B C   1 
ATOM   3856 O  O   . PHE B 1 206 ? -11.430 10.460  13.694  1.00 21.83 ? 206 PHE B O   1 
ATOM   3857 C  CB  . PHE B 1 206 ? -8.487  9.470   12.938  1.00 29.00 ? 206 PHE B CB  1 
ATOM   3858 C  CG  . PHE B 1 206 ? -7.466  10.427  12.344  1.00 34.67 ? 206 PHE B CG  1 
ATOM   3859 C  CD1 . PHE B 1 206 ? -6.458  10.991  13.142  1.00 39.64 ? 206 PHE B CD1 1 
ATOM   3860 C  CD2 . PHE B 1 206 ? -7.572  10.848  11.030  1.00 37.53 ? 206 PHE B CD2 1 
ATOM   3861 C  CE1 . PHE B 1 206 ? -5.579  11.946  12.632  1.00 44.06 ? 206 PHE B CE1 1 
ATOM   3862 C  CE2 . PHE B 1 206 ? -6.668  11.769  10.502  1.00 42.21 ? 206 PHE B CE2 1 
ATOM   3863 C  CZ  . PHE B 1 206 ? -5.679  12.317  11.293  1.00 46.29 ? 206 PHE B CZ  1 
ATOM   3864 N  N   . GLY B 1 207 ? -10.138 12.220  14.114  1.00 23.59 ? 207 GLY B N   1 
ATOM   3865 C  CA  . GLY B 1 207 ? -11.227 13.188  14.098  1.00 21.31 ? 207 GLY B CA  1 
ATOM   3866 C  C   . GLY B 1 207 ? -11.773 13.537  15.473  1.00 21.11 ? 207 GLY B C   1 
ATOM   3867 O  O   . GLY B 1 207 ? -12.266 14.636  15.606  1.00 22.84 ? 207 GLY B O   1 
ATOM   3868 N  N   . LYS B 1 208 ? -11.581 12.709  16.529  1.00 15.64 ? 208 LYS B N   1 
ATOM   3869 C  CA  . LYS B 1 208 ? -12.100 13.023  17.847  1.00 16.22 ? 208 LYS B CA  1 
ATOM   3870 C  C   . LYS B 1 208 ? -10.948 13.151  18.867  1.00 16.42 ? 208 LYS B C   1 
ATOM   3871 O  O   . LYS B 1 208 ? -11.117 13.780  19.916  1.00 19.20 ? 208 LYS B O   1 
ATOM   3872 C  CB  . LYS B 1 208 ? -13.083 11.965  18.328  1.00 18.71 ? 208 LYS B CB  1 
ATOM   3873 C  CG  . LYS B 1 208 ? -14.299 11.731  17.433  1.00 23.42 ? 208 LYS B CG  1 
ATOM   3874 C  CD  . LYS B 1 208 ? -15.178 10.631  18.002  1.00 28.93 ? 208 LYS B CD  1 
ATOM   3875 C  CE  . LYS B 1 208 ? -16.239 10.118  17.037  1.00 34.84 ? 208 LYS B CE  1 
ATOM   3876 N  NZ  . LYS B 1 208 ? -17.438 9.545   17.728  1.00 32.33 ? 208 LYS B NZ  1 
ATOM   3877 N  N   . VAL B 1 209 ? -9.858  12.406  18.637  1.00 15.34 ? 209 VAL B N   1 
ATOM   3878 C  CA  . VAL B 1 209 ? -8.649  12.450  19.456  1.00 12.97 ? 209 VAL B CA  1 
ATOM   3879 C  C   . VAL B 1 209 ? -7.420  12.509  18.538  1.00 12.59 ? 209 VAL B C   1 
ATOM   3880 O  O   . VAL B 1 209 ? -7.431  12.016  17.395  1.00 14.77 ? 209 VAL B O   1 
ATOM   3881 C  CB  . VAL B 1 209 ? -8.479  11.236  20.424  1.00 14.67 ? 209 VAL B CB  1 
ATOM   3882 C  CG1 . VAL B 1 209 ? -9.602  11.235  21.448  1.00 16.50 ? 209 VAL B CG1 1 
ATOM   3883 C  CG2 . VAL B 1 209 ? -8.371  9.878   19.714  1.00 14.74 ? 209 VAL B CG2 1 
ATOM   3884 N  N   . VAL B 1 210 ? -6.315  13.008  19.095  1.00 12.22 ? 210 VAL B N   1 
ATOM   3885 C  CA  . VAL B 1 210 ? -4.994  12.945  18.443  1.00 12.70 ? 210 VAL B CA  1 
ATOM   3886 C  C   . VAL B 1 210 ? -4.024  12.382  19.467  1.00 12.92 ? 210 VAL B C   1 
ATOM   3887 O  O   . VAL B 1 210 ? -4.238  12.525  20.655  1.00 15.10 ? 210 VAL B O   1 
ATOM   3888 C  CB  . VAL B 1 210 ? -4.478  14.323  18.003  1.00 16.21 ? 210 VAL B CB  1 
ATOM   3889 C  CG1 . VAL B 1 210 ? -5.229  14.765  16.739  1.00 19.53 ? 210 VAL B CG1 1 
ATOM   3890 C  CG2 . VAL B 1 210 ? -4.602  15.374  19.120  1.00 16.85 ? 210 VAL B CG2 1 
ATOM   3891 N  N   . VAL B 1 211 ? -2.920  11.838  19.014  1.00 12.68 ? 211 VAL B N   1 
ATOM   3892 C  CA  . VAL B 1 211 ? -1.884  11.362  19.917  1.00 14.47 ? 211 VAL B CA  1 
ATOM   3893 C  C   . VAL B 1 211 ? -0.988  12.531  20.253  1.00 15.89 ? 211 VAL B C   1 
ATOM   3894 O  O   . VAL B 1 211 ? -0.472  13.235  19.368  1.00 17.88 ? 211 VAL B O   1 
ATOM   3895 C  CB  . VAL B 1 211 ? -1.028  10.261  19.243  1.00 14.75 ? 211 VAL B CB  1 
ATOM   3896 C  CG1 . VAL B 1 211 ? -0.021  9.733   20.239  1.00 16.80 ? 211 VAL B CG1 1 
ATOM   3897 C  CG2 . VAL B 1 211 ? -1.877  9.155   18.659  1.00 15.20 ? 211 VAL B CG2 1 
ATOM   3898 N  N   . ARG B 1 212 ? -0.879  12.791  21.559  1.00 13.60 ? 212 ARG B N   1 
ATOM   3899 C  CA  . ARG B 1 212 ? -0.111  13.907  22.055  1.00 14.31 ? 212 ARG B CA  1 
ATOM   3900 C  C   . ARG B 1 212 ? 1.345   13.485  22.215  1.00 14.53 ? 212 ARG B C   1 
ATOM   3901 O  O   . ARG B 1 212 ? 2.264   14.156  21.724  1.00 13.34 ? 212 ARG B O   1 
ATOM   3902 C  CB  . ARG B 1 212 ? -0.717  14.417  23.364  1.00 14.01 ? 212 ARG B CB  1 
ATOM   3903 C  CG  . ARG B 1 212 ? 0.034   15.566  23.996  1.00 16.17 ? 212 ARG B CG  1 
ATOM   3904 C  CD  . ARG B 1 212 ? -0.506  15.899  25.371  1.00 14.52 ? 212 ARG B CD  1 
ATOM   3905 N  NE  . ARG B 1 212 ? 0.197   17.029  25.917  1.00 16.24 ? 212 ARG B NE  1 
ATOM   3906 C  CZ  . ARG B 1 212 ? 0.084   18.284  25.497  1.00 22.14 ? 212 ARG B CZ  1 
ATOM   3907 N  NH1 . ARG B 1 212 ? -0.913  18.637  24.688  1.00 21.75 ? 212 ARG B NH1 1 
ATOM   3908 N  NH2 . ARG B 1 212 ? 0.993   19.182  25.831  1.00 25.58 ? 212 ARG B NH2 1 
ATOM   3909 N  N   . TRP B 1 213 ? 1.575   12.332  22.879  1.00 13.02 ? 213 TRP B N   1 
ATOM   3910 C  CA  . TRP B 1 213 ? 2.918   11.795  22.986  1.00 12.69 ? 213 TRP B CA  1 
ATOM   3911 C  C   . TRP B 1 213 ? 2.807   10.286  23.186  1.00 12.66 ? 213 TRP B C   1 
ATOM   3912 O  O   . TRP B 1 213 ? 1.773   9.816   23.620  1.00 13.86 ? 213 TRP B O   1 
ATOM   3913 C  CB  . TRP B 1 213 ? 3.743   12.428  24.115  1.00 11.66 ? 213 TRP B CB  1 
ATOM   3914 C  CG  . TRP B 1 213 ? 3.155   12.423  25.496  1.00 13.03 ? 213 TRP B CG  1 
ATOM   3915 C  CD1 . TRP B 1 213 ? 2.457   13.420  26.101  1.00 13.06 ? 213 TRP B CD1 1 
ATOM   3916 C  CD2 . TRP B 1 213 ? 3.291   11.411  26.488  1.00 12.62 ? 213 TRP B CD2 1 
ATOM   3917 N  NE1 . TRP B 1 213 ? 2.074   13.069  27.370  1.00 14.31 ? 213 TRP B NE1 1 
ATOM   3918 C  CE2 . TRP B 1 213 ? 2.623   11.860  27.652  1.00 13.68 ? 213 TRP B CE2 1 
ATOM   3919 C  CE3 . TRP B 1 213 ? 3.967   10.183  26.516  1.00 16.33 ? 213 TRP B CE3 1 
ATOM   3920 C  CZ2 . TRP B 1 213 ? 2.548   11.094  28.807  1.00 14.74 ? 213 TRP B CZ2 1 
ATOM   3921 C  CZ3 . TRP B 1 213 ? 3.824   9.399   27.637  1.00 15.76 ? 213 TRP B CZ3 1 
ATOM   3922 C  CH2 . TRP B 1 213 ? 3.197   9.884   28.786  1.00 16.93 ? 213 TRP B CH2 1 
ATOM   3923 N  N   A SER B 1 214 ? 3.887   9.577   22.925  0.50 12.82 ? 214 SER B N   1 
ATOM   3924 N  N   B SER B 1 214 ? 3.901   9.560   22.908  0.50 13.48 ? 214 SER B N   1 
ATOM   3925 C  CA  A SER B 1 214 ? 3.885   8.154   23.166  0.50 13.11 ? 214 SER B CA  1 
ATOM   3926 C  CA  B SER B 1 214 ? 3.939   8.099   22.830  0.50 14.06 ? 214 SER B CA  1 
ATOM   3927 C  C   A SER B 1 214 ? 5.278   7.742   23.592  0.50 14.82 ? 214 SER B C   1 
ATOM   3928 C  C   B SER B 1 214 ? 5.301   7.592   23.316  0.50 15.81 ? 214 SER B C   1 
ATOM   3929 O  O   A SER B 1 214 ? 6.266   8.490   23.406  0.50 15.32 ? 214 SER B O   1 
ATOM   3930 O  O   B SER B 1 214 ? 6.328   8.152   22.881  0.50 17.03 ? 214 SER B O   1 
ATOM   3931 C  CB  A SER B 1 214 ? 3.440   7.368   21.985  0.50 13.14 ? 214 SER B CB  1 
ATOM   3932 C  CB  B SER B 1 214 ? 3.700   7.647   21.412  0.50 15.84 ? 214 SER B CB  1 
ATOM   3933 O  OG  A SER B 1 214 ? 4.342   7.547   20.879  0.50 13.91 ? 214 SER B OG  1 
ATOM   3934 O  OG  B SER B 1 214 ? 3.898   6.241   21.256  0.50 15.36 ? 214 SER B OG  1 
ATOM   3935 N  N   . GLN B 1 215 ? 5.318   6.563   24.192  1.00 12.56 ? 215 GLN B N   1 
ATOM   3936 C  CA  . GLN B 1 215 ? 6.571   6.043   24.728  1.00 13.52 ? 215 GLN B CA  1 
ATOM   3937 C  C   . GLN B 1 215 ? 6.573   4.524   24.582  1.00 12.46 ? 215 GLN B C   1 
ATOM   3938 O  O   . GLN B 1 215 ? 5.656   3.872   25.103  1.00 12.74 ? 215 GLN B O   1 
ATOM   3939 C  CB  . GLN B 1 215 ? 6.706   6.428   26.221  1.00 12.56 ? 215 GLN B CB  1 
ATOM   3940 C  CG  . GLN B 1 215 ? 8.031   5.955   26.821  1.00 14.01 ? 215 GLN B CG  1 
ATOM   3941 C  CD  . GLN B 1 215 ? 9.210   6.704   26.258  1.00 16.24 ? 215 GLN B CD  1 
ATOM   3942 O  OE1 . GLN B 1 215 ? 9.251   7.943   26.314  1.00 16.17 ? 215 GLN B OE1 1 
ATOM   3943 N  NE2 . GLN B 1 215 ? 10.130  5.980   25.609  1.00 16.05 ? 215 GLN B NE2 1 
ATOM   3944 N  N   . LEU B 1 216 ? 7.617   3.968   23.951  1.00 13.20 ? 216 LEU B N   1 
ATOM   3945 C  CA  . LEU B 1 216 ? 7.842   2.511   24.000  1.00 14.55 ? 216 LEU B CA  1 
ATOM   3946 C  C   . LEU B 1 216 ? 8.741   2.200   25.213  1.00 14.48 ? 216 LEU B C   1 
ATOM   3947 O  O   . LEU B 1 216 ? 9.706   2.927   25.453  1.00 17.42 ? 216 LEU B O   1 
ATOM   3948 C  CB  . LEU B 1 216 ? 8.538   2.137   22.676  1.00 18.74 ? 216 LEU B CB  1 
ATOM   3949 C  CG  . LEU B 1 216 ? 8.049   0.984   21.788  1.00 31.43 ? 216 LEU B CG  1 
ATOM   3950 C  CD1 . LEU B 1 216 ? 6.536   0.918   21.636  1.00 33.09 ? 216 LEU B CD1 1 
ATOM   3951 C  CD2 . LEU B 1 216 ? 8.677   1.142   20.397  1.00 32.83 ? 216 LEU B CD2 1 
ATOM   3952 N  N   . GLY B 1 217 ? 8.497   1.110   25.901  1.00 12.06 ? 217 GLY B N   1 
ATOM   3953 C  CA  . GLY B 1 217 ? 9.340   0.577   26.941  1.00 13.24 ? 217 GLY B CA  1 
ATOM   3954 C  C   . GLY B 1 217 ? 9.522   -0.955  26.867  1.00 15.79 ? 217 GLY B C   1 
ATOM   3955 O  O   . GLY B 1 217 ? 8.788   -1.647  26.207  1.00 12.26 ? 217 GLY B O   1 
ATOM   3956 N  N   . PHE B 1 218 ? 10.483  -1.481  27.664  1.00 17.64 ? 218 PHE B N   1 
ATOM   3957 C  CA  . PHE B 1 218 ? 10.887  -2.888  27.793  1.00 17.70 ? 218 PHE B CA  1 
ATOM   3958 C  C   . PHE B 1 218 ? 11.206  -3.149  29.276  1.00 17.62 ? 218 PHE B C   1 
ATOM   3959 O  O   . PHE B 1 218 ? 11.573  -2.275  30.081  1.00 14.99 ? 218 PHE B O   1 
ATOM   3960 C  CB  . PHE B 1 218 ? 11.893  -3.355  26.720  1.00 17.04 ? 218 PHE B CB  1 
ATOM   3961 C  CG  . PHE B 1 218 ? 13.231  -2.647  26.796  1.00 22.99 ? 218 PHE B CG  1 
ATOM   3962 C  CD1 . PHE B 1 218 ? 14.196  -3.046  27.702  1.00 18.13 ? 218 PHE B CD1 1 
ATOM   3963 C  CD2 . PHE B 1 218 ? 13.512  -1.550  25.977  1.00 21.12 ? 218 PHE B CD2 1 
ATOM   3964 C  CE1 . PHE B 1 218 ? 15.431  -2.375  27.797  1.00 18.41 ? 218 PHE B CE1 1 
ATOM   3965 C  CE2 . PHE B 1 218 ? 14.692  -0.850  26.113  1.00 22.68 ? 218 PHE B CE2 1 
ATOM   3966 C  CZ  . PHE B 1 218 ? 15.657  -1.264  27.046  1.00 18.63 ? 218 PHE B CZ  1 
ATOM   3967 N  N   . GLY B 1 219 ? 10.873  -4.357  29.683  1.00 19.54 ? 219 GLY B N   1 
ATOM   3968 C  CA  . GLY B 1 219 ? 11.262  -4.879  30.966  1.00 19.78 ? 219 GLY B CA  1 
ATOM   3969 C  C   . GLY B 1 219 ? 12.056  -6.148  30.626  1.00 21.91 ? 219 GLY B C   1 
ATOM   3970 O  O   . GLY B 1 219 ? 13.071  -6.068  29.933  1.00 26.01 ? 219 GLY B O   1 
ATOM   3971 N  N   . LYS B 1 220 ? 11.659  -7.294  31.197  1.00 24.43 ? 220 LYS B N   1 
ATOM   3972 C  CA  . LYS B 1 220 ? 12.373  -8.538  30.932  1.00 26.47 ? 220 LYS B CA  1 
ATOM   3973 C  C   . LYS B 1 220 ? 11.852  -9.149  29.633  1.00 21.52 ? 220 LYS B C   1 
ATOM   3974 O  O   . LYS B 1 220 ? 10.767  -8.778  29.142  1.00 23.82 ? 220 LYS B O   1 
ATOM   3975 C  CB  . LYS B 1 220 ? 12.049  -9.594  32.004  1.00 33.56 ? 220 LYS B CB  1 
ATOM   3976 C  CG  . LYS B 1 220 ? 12.533  -9.329  33.417  1.00 37.64 ? 220 LYS B CG  1 
ATOM   3977 C  CD  . LYS B 1 220 ? 11.657  -10.041 34.486  1.00 47.19 ? 220 LYS B CD  1 
ATOM   3978 C  CE  . LYS B 1 220 ? 11.667  -11.558 34.464  1.00 51.55 ? 220 LYS B CE  1 
ATOM   3979 N  NZ  . LYS B 1 220 ? 11.122  -12.140 33.202  1.00 52.59 ? 220 LYS B NZ  1 
ATOM   3980 N  N   . THR B 1 221 ? 12.593  -10.138 29.113  1.00 22.27 ? 221 THR B N   1 
ATOM   3981 C  CA  . THR B 1 221 ? 12.141  -10.979 28.013  1.00 21.04 ? 221 THR B CA  1 
ATOM   3982 C  C   . THR B 1 221 ? 11.845  -12.362 28.628  1.00 24.77 ? 221 THR B C   1 
ATOM   3983 O  O   . THR B 1 221 ? 12.753  -13.052 29.141  1.00 26.96 ? 221 THR B O   1 
ATOM   3984 C  CB  . THR B 1 221 ? 13.195  -11.013 26.891  1.00 24.36 ? 221 THR B CB  1 
ATOM   3985 O  OG1 . THR B 1 221 ? 13.383  -9.655  26.459  1.00 23.81 ? 221 THR B OG1 1 
ATOM   3986 C  CG2 . THR B 1 221 ? 12.795  -11.912 25.733  1.00 20.30 ? 221 THR B CG2 1 
ATOM   3987 N  N   . SER B 1 222 ? 10.562  -12.713 28.678  1.00 26.54 ? 222 SER B N   1 
ATOM   3988 C  CA  . SER B 1 222 ? 10.074  -13.852 29.468  1.00 28.74 ? 222 SER B CA  1 
ATOM   3989 C  C   . SER B 1 222 ? 10.496  -15.210 28.877  1.00 37.55 ? 222 SER B C   1 
ATOM   3990 O  O   . SER B 1 222 ? 10.567  -16.210 29.589  1.00 45.01 ? 222 SER B O   1 
ATOM   3991 C  CB  . SER B 1 222 ? 8.566   -13.791 29.597  1.00 29.30 ? 222 SER B CB  1 
ATOM   3992 O  OG  . SER B 1 222 ? 8.237   -12.825 30.562  1.00 27.05 ? 222 SER B OG  1 
ATOM   3993 N  N   . SER B 1 223 ? 10.806  -15.240 27.572  1.00 32.82 ? 223 SER B N   1 
ATOM   3994 C  CA  . SER B 1 223 ? 11.167  -16.496 26.917  1.00 34.58 ? 223 SER B CA  1 
ATOM   3995 C  C   . SER B 1 223 ? 12.550  -16.970 27.391  1.00 43.19 ? 223 SER B C   1 
ATOM   3996 O  O   . SER B 1 223 ? 12.846  -18.161 27.284  1.00 43.37 ? 223 SER B O   1 
ATOM   3997 C  CB  . SER B 1 223 ? 11.086  -16.360 25.398  1.00 35.38 ? 223 SER B CB  1 
ATOM   3998 O  OG  . SER B 1 223 ? 12.133  -15.519 24.882  1.00 38.02 ? 223 SER B OG  1 
ATOM   3999 N  N   . THR B 1 224 ? 13.391  -16.041 27.898  1.00 36.31 ? 224 THR B N   1 
ATOM   4000 C  CA  . THR B 1 224 ? 14.788  -16.316 28.206  1.00 40.40 ? 224 THR B CA  1 
ATOM   4001 C  C   . THR B 1 224 ? 15.091  -16.072 29.702  1.00 37.62 ? 224 THR B C   1 
ATOM   4002 O  O   . THR B 1 224 ? 16.152  -16.477 30.184  1.00 39.96 ? 224 THR B O   1 
ATOM   4003 C  CB  . THR B 1 224 ? 15.692  -15.467 27.284  1.00 43.97 ? 224 THR B CB  1 
ATOM   4004 O  OG1 . THR B 1 224 ? 15.400  -14.082 27.495  1.00 48.47 ? 224 THR B OG1 1 
ATOM   4005 C  CG2 . THR B 1 224 ? 15.501  -15.749 25.810  1.00 48.19 ? 224 THR B CG2 1 
ATOM   4006 N  N   . THR B 1 225 ? 14.153  -15.473 30.466  1.00 32.59 ? 225 THR B N   1 
ATOM   4007 C  CA  . THR B 1 225 ? 14.427  -14.956 31.803  1.00 38.06 ? 225 THR B CA  1 
ATOM   4008 C  C   . THR B 1 225 ? 13.322  -15.454 32.749  1.00 41.98 ? 225 THR B C   1 
ATOM   4009 O  O   . THR B 1 225 ? 12.140  -15.188 32.473  1.00 42.07 ? 225 THR B O   1 
ATOM   4010 C  CB  . THR B 1 225 ? 14.461  -13.412 31.789  1.00 36.16 ? 225 THR B CB  1 
ATOM   4011 O  OG1 . THR B 1 225 ? 15.056  -12.870 30.605  1.00 34.68 ? 225 THR B OG1 1 
ATOM   4012 C  CG2 . THR B 1 225 ? 15.139  -12.835 33.013  1.00 43.31 ? 225 THR B CG2 1 
ATOM   4013 N  N   . PRO B 1 226 ? 13.624  -16.147 33.892  1.00 43.44 ? 226 PRO B N   1 
ATOM   4014 C  CA  . PRO B 1 226 ? 12.560  -16.653 34.781  1.00 44.80 ? 226 PRO B CA  1 
ATOM   4015 C  C   . PRO B 1 226 ? 11.762  -15.488 35.380  1.00 51.61 ? 226 PRO B C   1 
ATOM   4016 O  O   . PRO B 1 226 ? 12.327  -14.395 35.543  1.00 40.02 ? 226 PRO B O   1 
ATOM   4017 C  CB  . PRO B 1 226 ? 13.297  -17.485 35.858  1.00 44.06 ? 226 PRO B CB  1 
ATOM   4018 C  CG  . PRO B 1 226 ? 14.694  -17.686 35.294  1.00 42.53 ? 226 PRO B CG  1 
ATOM   4019 C  CD  . PRO B 1 226 ? 14.970  -16.481 34.393  1.00 41.64 ? 226 PRO B CD  1 
ATOM   4020 N  N   . ASP B 1 227 ? 10.455  -15.696 35.630  1.00 49.40 ? 227 ASP B N   1 
ATOM   4021 C  CA  . ASP B 1 227 ? 9.579   -14.581 35.978  1.00 59.62 ? 227 ASP B CA  1 
ATOM   4022 C  C   . ASP B 1 227 ? 9.726   -14.204 37.462  1.00 53.13 ? 227 ASP B C   1 
ATOM   4023 O  O   . ASP B 1 227 ? 9.281   -13.127 37.849  1.00 47.61 ? 227 ASP B O   1 
ATOM   4024 C  CB  . ASP B 1 227 ? 8.103   -14.827 35.637  1.00 60.99 ? 227 ASP B CB  1 
ATOM   4025 C  CG  . ASP B 1 227 ? 7.543   -15.896 36.537  1.00 67.40 ? 227 ASP B CG  1 
ATOM   4026 O  OD1 . ASP B 1 227 ? 7.714   -17.066 36.183  1.00 80.98 ? 227 ASP B OD1 1 
ATOM   4027 O  OD2 . ASP B 1 227 ? 7.086   -15.545 37.649  1.00 72.87 ? 227 ASP B OD2 1 
ATOM   4028 N  N   . LYS B 1 228 ? 10.341  -15.056 38.300  1.00 48.38 ? 228 LYS B N   1 
ATOM   4029 C  CA  . LYS B 1 228 ? 10.546  -14.691 39.695  1.00 47.98 ? 228 LYS B CA  1 
ATOM   4030 C  C   . LYS B 1 228 ? 11.930  -14.005 39.833  1.00 44.99 ? 228 LYS B C   1 
ATOM   4031 O  O   . LYS B 1 228 ? 12.377  -13.680 40.937  1.00 53.35 ? 228 LYS B O   1 
ATOM   4032 C  CB  . LYS B 1 228 ? 10.302  -15.932 40.586  1.00 42.89 ? 228 LYS B CB  1 
ATOM   4033 C  CG  . LYS B 1 228 ? 8.925   -16.043 41.268  1.00 41.62 ? 228 LYS B CG  1 
ATOM   4034 N  N   . GLN B 1 229 ? 12.644  -13.809 38.712  1.00 38.88 ? 229 GLN B N   1 
ATOM   4035 C  CA  . GLN B 1 229 ? 13.862  -13.011 38.727  1.00 34.05 ? 229 GLN B CA  1 
ATOM   4036 C  C   . GLN B 1 229 ? 13.481  -11.521 38.667  1.00 26.73 ? 229 GLN B C   1 
ATOM   4037 O  O   . GLN B 1 229 ? 12.699  -11.076 37.840  1.00 27.72 ? 229 GLN B O   1 
ATOM   4038 C  CB  . GLN B 1 229 ? 14.772  -13.454 37.588  1.00 31.23 ? 229 GLN B CB  1 
ATOM   4039 C  CG  . GLN B 1 229 ? 16.145  -12.771 37.591  1.00 35.77 ? 229 GLN B CG  1 
ATOM   4040 C  CD  . GLN B 1 229 ? 17.029  -13.483 36.582  1.00 37.69 ? 229 GLN B CD  1 
ATOM   4041 O  OE1 . GLN B 1 229 ? 17.194  -14.698 36.666  1.00 44.86 ? 229 GLN B OE1 1 
ATOM   4042 N  NE2 . GLN B 1 229 ? 17.557  -12.759 35.598  1.00 31.62 ? 229 GLN B NE2 1 
ATOM   4043 N  N   . THR B 1 230 ? 14.094  -10.700 39.526  1.00 25.21 ? 230 THR B N   1 
ATOM   4044 C  CA  . THR B 1 230 ? 13.861  -9.262  39.466  1.00 25.35 ? 230 THR B CA  1 
ATOM   4045 C  C   . THR B 1 230 ? 14.551  -8.697  38.228  1.00 19.99 ? 230 THR B C   1 
ATOM   4046 O  O   . THR B 1 230 ? 15.737  -8.980  38.013  1.00 21.25 ? 230 THR B O   1 
ATOM   4047 C  CB  . THR B 1 230 ? 14.438  -8.556  40.713  1.00 23.66 ? 230 THR B CB  1 
ATOM   4048 O  OG1 . THR B 1 230 ? 13.983  -9.388  41.793  1.00 26.08 ? 230 THR B OG1 1 
ATOM   4049 C  CG2 . THR B 1 230 ? 13.957  -7.110  40.821  1.00 22.38 ? 230 THR B CG2 1 
ATOM   4050 N  N   . PRO B 1 231 ? 13.886  -7.886  37.391  1.00 21.59 ? 231 PRO B N   1 
ATOM   4051 C  CA  . PRO B 1 231 ? 14.589  -7.269  36.263  1.00 20.79 ? 231 PRO B CA  1 
ATOM   4052 C  C   . PRO B 1 231 ? 15.581  -6.225  36.789  1.00 20.88 ? 231 PRO B C   1 
ATOM   4053 O  O   . PRO B 1 231 ? 15.397  -5.632  37.869  1.00 19.17 ? 231 PRO B O   1 
ATOM   4054 C  CB  . PRO B 1 231 ? 13.526  -6.541  35.443  1.00 24.66 ? 231 PRO B CB  1 
ATOM   4055 C  CG  . PRO B 1 231 ? 12.329  -6.407  36.388  1.00 26.40 ? 231 PRO B CG  1 
ATOM   4056 C  CD  . PRO B 1 231 ? 12.498  -7.455  37.480  1.00 23.62 ? 231 PRO B CD  1 
ATOM   4057 N  N   . ARG B 1 232 ? 16.557  -5.904  35.950  1.00 21.19 ? 232 ARG B N   1 
ATOM   4058 C  CA  . ARG B 1 232 ? 17.459  -4.810  36.254  1.00 19.19 ? 232 ARG B CA  1 
ATOM   4059 C  C   . ARG B 1 232 ? 17.097  -3.593  35.409  1.00 18.74 ? 232 ARG B C   1 
ATOM   4060 O  O   . ARG B 1 232 ? 16.696  -3.701  34.269  1.00 16.68 ? 232 ARG B O   1 
ATOM   4061 C  CB  . ARG B 1 232 ? 18.923  -5.200  36.045  1.00 21.11 ? 232 ARG B CB  1 
ATOM   4062 C  CG  . ARG B 1 232 ? 19.433  -6.214  37.044  1.00 21.45 ? 232 ARG B CG  1 
ATOM   4063 C  CD  . ARG B 1 232 ? 20.841  -6.639  36.737  1.00 23.63 ? 232 ARG B CD  1 
ATOM   4064 N  NE  . ARG B 1 232 ? 21.140  -7.652  37.743  1.00 20.22 ? 232 ARG B NE  1 
ATOM   4065 C  CZ  . ARG B 1 232 ? 21.955  -7.510  38.769  1.00 22.50 ? 232 ARG B CZ  1 
ATOM   4066 N  NH1 . ARG B 1 232 ? 22.340  -6.315  39.196  1.00 21.81 ? 232 ARG B NH1 1 
ATOM   4067 N  NH2 . ARG B 1 232 ? 22.273  -8.586  39.458  1.00 23.68 ? 232 ARG B NH2 1 
ATOM   4068 N  N   . ASN B 1 233 ? 17.234  -2.413  36.004  1.00 17.45 ? 233 ASN B N   1 
ATOM   4069 C  CA  . ASN B 1 233 ? 17.076  -1.183  35.257  1.00 15.55 ? 233 ASN B CA  1 
ATOM   4070 C  C   . ASN B 1 233 ? 18.405  -0.915  34.516  1.00 13.84 ? 233 ASN B C   1 
ATOM   4071 O  O   . ASN B 1 233 ? 19.366  -1.647  34.656  1.00 14.58 ? 233 ASN B O   1 
ATOM   4072 C  CB  . ASN B 1 233 ? 16.608  -0.028  36.147  1.00 15.74 ? 233 ASN B CB  1 
ATOM   4073 C  CG  . ASN B 1 233 ? 17.588  0.276   37.268  1.00 18.76 ? 233 ASN B CG  1 
ATOM   4074 O  OD1 . ASN B 1 233 ? 18.800  0.224   37.068  1.00 14.76 ? 233 ASN B OD1 1 
ATOM   4075 N  ND2 . ASN B 1 233 ? 17.075  0.480   38.469  1.00 22.15 ? 233 ASN B ND2 1 
ATOM   4076 N  N   . LEU B 1 234 ? 18.471  0.187   33.759  1.00 12.89 ? 234 LEU B N   1 
ATOM   4077 C  CA  . LEU B 1 234 ? 19.608  0.466   32.916  1.00 12.74 ? 234 LEU B CA  1 
ATOM   4078 C  C   . LEU B 1 234 ? 20.770  1.036   33.709  1.00 14.51 ? 234 LEU B C   1 
ATOM   4079 O  O   . LEU B 1 234 ? 21.832  1.215   33.137  1.00 15.82 ? 234 LEU B O   1 
ATOM   4080 C  CB  . LEU B 1 234 ? 19.198  1.390   31.782  1.00 14.57 ? 234 LEU B CB  1 
ATOM   4081 C  CG  . LEU B 1 234 ? 18.189  0.725   30.813  1.00 18.78 ? 234 LEU B CG  1 
ATOM   4082 C  CD1 . LEU B 1 234 ? 17.899  1.660   29.664  1.00 21.78 ? 234 LEU B CD1 1 
ATOM   4083 C  CD2 . LEU B 1 234 ? 18.660  -0.620  30.313  1.00 20.24 ? 234 LEU B CD2 1 
ATOM   4084 N  N   . LEU B 1 235 ? 20.611  1.207   35.009  1.00 15.90 ? 235 LEU B N   1 
ATOM   4085 C  CA  . LEU B 1 235 ? 21.787  1.522   35.832  1.00 13.85 ? 235 LEU B CA  1 
ATOM   4086 C  C   . LEU B 1 235 ? 22.448  0.233   36.321  1.00 15.99 ? 235 LEU B C   1 
ATOM   4087 O  O   . LEU B 1 235 ? 23.464  0.288   37.038  1.00 15.81 ? 235 LEU B O   1 
ATOM   4088 C  CB  . LEU B 1 235 ? 21.379  2.404   37.010  1.00 14.61 ? 235 LEU B CB  1 
ATOM   4089 C  CG  . LEU B 1 235 ? 20.778  3.751   36.644  1.00 15.62 ? 235 LEU B CG  1 
ATOM   4090 C  CD1 . LEU B 1 235 ? 20.453  4.525   37.899  1.00 17.20 ? 235 LEU B CD1 1 
ATOM   4091 C  CD2 . LEU B 1 235 ? 21.695  4.550   35.752  1.00 16.63 ? 235 LEU B CD2 1 
ATOM   4092 N  N   . GLY B 1 236 ? 21.845  -0.927  35.973  1.00 13.97 ? 236 GLY B N   1 
ATOM   4093 C  CA  . GLY B 1 236 ? 22.366  -2.246  36.297  1.00 13.64 ? 236 GLY B CA  1 
ATOM   4094 C  C   . GLY B 1 236 ? 21.971  -2.771  37.689  1.00 13.90 ? 236 GLY B C   1 
ATOM   4095 O  O   . GLY B 1 236 ? 22.540  -3.744  38.139  1.00 16.56 ? 236 GLY B O   1 
ATOM   4096 N  N   . PHE B 1 237 ? 21.014  -2.108  38.367  1.00 14.00 ? 237 PHE B N   1 
ATOM   4097 C  CA  . PHE B 1 237 ? 20.500  -2.535  39.659  1.00 14.56 ? 237 PHE B CA  1 
ATOM   4098 C  C   . PHE B 1 237 ? 19.151  -3.237  39.495  1.00 15.58 ? 237 PHE B C   1 
ATOM   4099 O  O   . PHE B 1 237 ? 18.323  -2.819  38.671  1.00 15.76 ? 237 PHE B O   1 
ATOM   4100 C  CB  . PHE B 1 237 ? 20.369  -1.365  40.661  1.00 15.39 ? 237 PHE B CB  1 
ATOM   4101 C  CG  . PHE B 1 237 ? 21.664  -0.937  41.289  1.00 14.64 ? 237 PHE B CG  1 
ATOM   4102 C  CD1 . PHE B 1 237 ? 22.625  -0.238  40.585  1.00 15.21 ? 237 PHE B CD1 1 
ATOM   4103 C  CD2 . PHE B 1 237 ? 21.960  -1.266  42.620  1.00 16.72 ? 237 PHE B CD2 1 
ATOM   4104 C  CE1 . PHE B 1 237 ? 23.841  0.077   41.167  1.00 13.91 ? 237 PHE B CE1 1 
ATOM   4105 C  CE2 . PHE B 1 237 ? 23.171  -0.924  43.196  1.00 14.92 ? 237 PHE B CE2 1 
ATOM   4106 C  CZ  . PHE B 1 237 ? 24.109  -0.289  42.458  1.00 15.16 ? 237 PHE B CZ  1 
ATOM   4107 N  N   . LYS B 1 238 ? 18.940  -4.276  40.321  1.00 16.64 ? 238 LYS B N   1 
ATOM   4108 C  CA  . LYS B 1 238 ? 17.642  -4.922  40.377  1.00 17.10 ? 238 LYS B CA  1 
ATOM   4109 C  C   . LYS B 1 238 ? 16.623  -3.857  40.777  1.00 17.25 ? 238 LYS B C   1 
ATOM   4110 O  O   . LYS B 1 238 ? 16.924  -3.036  41.678  1.00 16.70 ? 238 LYS B O   1 
ATOM   4111 C  CB  . LYS B 1 238 ? 17.681  -6.077  41.377  1.00 19.01 ? 238 LYS B CB  1 
ATOM   4112 C  CG  . LYS B 1 238 ? 18.639  -7.200  41.016  1.00 20.02 ? 238 LYS B CG  1 
ATOM   4113 C  CD  . LYS B 1 238 ? 18.484  -8.357  41.951  1.00 21.88 ? 238 LYS B CD  1 
ATOM   4114 C  CE  . LYS B 1 238 ? 19.479  -9.471  41.696  1.00 21.90 ? 238 LYS B CE  1 
ATOM   4115 N  NZ  . LYS B 1 238 ? 19.483  -10.412 42.828  1.00 21.97 ? 238 LYS B NZ  1 
ATOM   4116 N  N   . ASP B 1 239 ? 15.447  -3.908  40.165  1.00 16.14 ? 239 ASP B N   1 
ATOM   4117 C  CA  . ASP B 1 239 ? 14.433  -2.877  40.304  1.00 16.36 ? 239 ASP B CA  1 
ATOM   4118 C  C   . ASP B 1 239 ? 13.084  -3.586  40.475  1.00 17.63 ? 239 ASP B C   1 
ATOM   4119 O  O   . ASP B 1 239 ? 12.597  -4.218  39.546  1.00 18.98 ? 239 ASP B O   1 
ATOM   4120 C  CB  . ASP B 1 239 ? 14.500  -1.870  39.130  1.00 16.61 ? 239 ASP B CB  1 
ATOM   4121 C  CG  . ASP B 1 239 ? 13.836  -0.531  39.391  1.00 19.13 ? 239 ASP B CG  1 
ATOM   4122 O  OD1 . ASP B 1 239 ? 12.887  -0.464  40.144  1.00 20.56 ? 239 ASP B OD1 1 
ATOM   4123 O  OD2 . ASP B 1 239 ? 14.249  0.453   38.767  1.00 19.90 ? 239 ASP B OD2 1 
ATOM   4124 N  N   . GLY B 1 240 ? 12.527  -3.527  41.681  1.00 16.04 ? 240 GLY B N   1 
ATOM   4125 C  CA  . GLY B 1 240 ? 11.169  -3.979  41.956  1.00 15.57 ? 240 GLY B CA  1 
ATOM   4126 C  C   . GLY B 1 240 ? 11.122  -4.890  43.184  1.00 17.05 ? 240 GLY B C   1 
ATOM   4127 O  O   . GLY B 1 240 ? 10.066  -5.456  43.448  1.00 18.41 ? 240 GLY B O   1 
ATOM   4128 N  N   . THR B 1 241 ? 12.267  -5.119  43.858  1.00 15.40 ? 241 THR B N   1 
ATOM   4129 C  CA  . THR B 1 241 ? 12.365  -6.042  44.958  1.00 17.25 ? 241 THR B CA  1 
ATOM   4130 C  C   . THR B 1 241 ? 11.294  -5.780  46.022  1.00 16.59 ? 241 THR B C   1 
ATOM   4131 O  O   . THR B 1 241 ? 10.554  -6.718  46.393  1.00 19.77 ? 241 THR B O   1 
ATOM   4132 C  CB  . THR B 1 241 ? 13.762  -5.979  45.624  1.00 17.88 ? 241 THR B CB  1 
ATOM   4133 O  OG1 . THR B 1 241 ? 14.780  -6.227  44.648  1.00 16.29 ? 241 THR B OG1 1 
ATOM   4134 C  CG2 . THR B 1 241 ? 13.884  -6.859  46.844  1.00 17.37 ? 241 THR B CG2 1 
ATOM   4135 N  N   . ARG B 1 242 ? 11.172  -4.509  46.482  1.00 14.63 ? 242 ARG B N   1 
ATOM   4136 C  CA  . ARG B 1 242 ? 10.171  -4.159  47.484  1.00 14.19 ? 242 ARG B CA  1 
ATOM   4137 C  C   . ARG B 1 242 ? 9.094   -3.322  46.837  1.00 17.43 ? 242 ARG B C   1 
ATOM   4138 O  O   . ARG B 1 242 ? 9.224   -2.106  46.724  1.00 17.20 ? 242 ARG B O   1 
ATOM   4139 C  CB  . ARG B 1 242 ? 10.774  -3.416  48.676  1.00 14.22 ? 242 ARG B CB  1 
ATOM   4140 C  CG  . ARG B 1 242 ? 11.402  -4.386  49.673  1.00 19.06 ? 242 ARG B CG  1 
ATOM   4141 C  CD  . ARG B 1 242 ? 12.062  -3.745  50.870  1.00 17.61 ? 242 ARG B CD  1 
ATOM   4142 N  NE  . ARG B 1 242 ? 11.263  -2.700  51.430  1.00 17.01 ? 242 ARG B NE  1 
ATOM   4143 C  CZ  . ARG B 1 242 ? 10.123  -2.809  52.053  1.00 19.29 ? 242 ARG B CZ  1 
ATOM   4144 N  NH1 . ARG B 1 242 ? 9.356   -1.732  52.145  1.00 19.38 ? 242 ARG B NH1 1 
ATOM   4145 N  NH2 . ARG B 1 242 ? 9.778   -3.983  52.596  1.00 23.05 ? 242 ARG B NH2 1 
ATOM   4146 N  N   . ASN B 1 243 ? 8.070   -4.012  46.340  1.00 16.44 ? 243 ASN B N   1 
ATOM   4147 C  CA  . ASN B 1 243 ? 6.990   -3.372  45.614  1.00 18.53 ? 243 ASN B CA  1 
ATOM   4148 C  C   . ASN B 1 243 ? 5.730   -4.069  46.103  1.00 21.35 ? 243 ASN B C   1 
ATOM   4149 O  O   . ASN B 1 243 ? 5.856   -5.193  46.598  1.00 25.60 ? 243 ASN B O   1 
ATOM   4150 C  CB  . ASN B 1 243 ? 7.238   -3.547  44.120  1.00 17.72 ? 243 ASN B CB  1 
ATOM   4151 C  CG  . ASN B 1 243 ? 6.374   -2.707  43.213  1.00 17.76 ? 243 ASN B CG  1 
ATOM   4152 O  OD1 . ASN B 1 243 ? 5.784   -1.697  43.581  1.00 16.20 ? 243 ASN B OD1 1 
ATOM   4153 N  ND2 . ASN B 1 243 ? 6.277   -3.122  41.973  1.00 18.90 ? 243 ASN B ND2 1 
ATOM   4154 N  N   . ILE B 1 244 ? 4.547   -3.538  45.758  1.00 19.66 ? 244 ILE B N   1 
ATOM   4155 C  CA  . ILE B 1 244 ? 3.306   -4.258  45.937  1.00 17.44 ? 244 ILE B CA  1 
ATOM   4156 C  C   . ILE B 1 244 ? 3.191   -5.289  44.820  1.00 18.72 ? 244 ILE B C   1 
ATOM   4157 O  O   . ILE B 1 244 ? 3.388   -4.936  43.643  1.00 20.71 ? 244 ILE B O   1 
ATOM   4158 C  CB  . ILE B 1 244 ? 2.141   -3.269  45.990  1.00 17.62 ? 244 ILE B CB  1 
ATOM   4159 C  CG1 . ILE B 1 244 ? 2.304   -2.265  47.141  1.00 17.15 ? 244 ILE B CG1 1 
ATOM   4160 C  CG2 . ILE B 1 244 ? 0.796   -3.992  46.108  1.00 20.72 ? 244 ILE B CG2 1 
ATOM   4161 C  CD1 . ILE B 1 244 ? 1.269   -1.227  47.093  1.00 18.82 ? 244 ILE B CD1 1 
ATOM   4162 N  N   . ALA B 1 245 ? 2.955   -6.541  45.205  1.00 19.89 ? 245 ALA B N   1 
ATOM   4163 C  CA  . ALA B 1 245 ? 2.721   -7.597  44.235  1.00 20.74 ? 245 ALA B CA  1 
ATOM   4164 C  C   . ALA B 1 245 ? 1.234   -7.762  43.989  1.00 19.42 ? 245 ALA B C   1 
ATOM   4165 O  O   . ALA B 1 245 ? 0.377   -7.470  44.810  1.00 18.87 ? 245 ALA B O   1 
ATOM   4166 C  CB  . ALA B 1 245 ? 3.358   -8.865  44.726  1.00 23.79 ? 245 ALA B CB  1 
ATOM   4167 N  N   . GLY B 1 246 ? 0.895   -8.174  42.760  1.00 22.46 ? 246 GLY B N   1 
ATOM   4168 C  CA  . GLY B 1 246 ? -0.518  -8.358  42.439  1.00 22.44 ? 246 GLY B CA  1 
ATOM   4169 C  C   . GLY B 1 246 ? -1.205  -9.494  43.183  1.00 21.69 ? 246 GLY B C   1 
ATOM   4170 O  O   . GLY B 1 246 ? -2.444  -9.485  43.245  1.00 24.45 ? 246 GLY B O   1 
ATOM   4171 N  N   . THR B 1 247 ? -0.432  -10.348 43.860  1.00 22.41 ? 247 THR B N   1 
ATOM   4172 C  CA  . THR B 1 247 ? -0.980  -11.333 44.801  1.00 23.67 ? 247 THR B CA  1 
ATOM   4173 C  C   . THR B 1 247 ? -1.489  -10.781 46.137  1.00 20.79 ? 247 THR B C   1 
ATOM   4174 O  O   . THR B 1 247 ? -2.173  -11.489 46.886  1.00 19.06 ? 247 THR B O   1 
ATOM   4175 C  CB  . THR B 1 247 ? 0.094   -12.391 45.100  1.00 29.03 ? 247 THR B CB  1 
ATOM   4176 O  OG1 . THR B 1 247 ? 1.262   -11.733 45.596  1.00 29.43 ? 247 THR B OG1 1 
ATOM   4177 C  CG2 . THR B 1 247 ? 0.568   -13.093 43.848  1.00 31.59 ? 247 THR B CG2 1 
ATOM   4178 N  N   . GLU B 1 248 ? -1.065  -9.556  46.529  1.00 19.12 ? 248 GLU B N   1 
ATOM   4179 C  CA  . GLU B 1 248 ? -1.318  -8.990  47.857  1.00 17.57 ? 248 GLU B CA  1 
ATOM   4180 C  C   . GLU B 1 248 ? -2.594  -8.170  47.867  1.00 18.95 ? 248 GLU B C   1 
ATOM   4181 O  O   . GLU B 1 248 ? -2.573  -6.912  47.798  1.00 15.35 ? 248 GLU B O   1 
ATOM   4182 C  CB  . GLU B 1 248 ? -0.147  -8.048  48.177  1.00 20.33 ? 248 GLU B CB  1 
ATOM   4183 C  CG  . GLU B 1 248 ? 1.181   -8.791  48.157  1.00 20.89 ? 248 GLU B CG  1 
ATOM   4184 C  CD  . GLU B 1 248 ? 2.342   -7.957  48.644  1.00 25.32 ? 248 GLU B CD  1 
ATOM   4185 O  OE1 . GLU B 1 248 ? 2.584   -8.064  49.814  1.00 34.48 ? 248 GLU B OE1 1 
ATOM   4186 O  OE2 . GLU B 1 248 ? 2.826   -7.089  47.958  1.00 20.24 ? 248 GLU B OE2 1 
ATOM   4187 N  N   . LYS B 1 249 ? -3.727  -8.912  47.900  1.00 17.71 ? 249 LYS B N   1 
ATOM   4188 C  CA  . LYS B 1 249 ? -5.055  -8.361  47.697  1.00 21.01 ? 249 LYS B CA  1 
ATOM   4189 C  C   . LYS B 1 249 ? -5.300  -7.264  48.728  1.00 19.27 ? 249 LYS B C   1 
ATOM   4190 O  O   . LYS B 1 249 ? -5.819  -6.193  48.394  1.00 18.08 ? 249 LYS B O   1 
ATOM   4191 C  CB  . LYS B 1 249 ? -6.084  -9.489  47.733  1.00 25.19 ? 249 LYS B CB  1 
ATOM   4192 C  CG  . LYS B 1 249 ? -5.993  -10.413 46.507  1.00 33.69 ? 249 LYS B CG  1 
ATOM   4193 N  N   . ASP B 1 250 ? -4.865  -7.473  49.994  1.00 21.49 ? 250 ASP B N   1 
ATOM   4194 C  CA  . ASP B 1 250 ? -5.170  -6.487  51.028  1.00 19.89 ? 250 ASP B CA  1 
ATOM   4195 C  C   . ASP B 1 250 ? -4.312  -5.218  50.883  1.00 16.22 ? 250 ASP B C   1 
ATOM   4196 O  O   . ASP B 1 250 ? -4.851  -4.111  51.091  1.00 18.99 ? 250 ASP B O   1 
ATOM   4197 C  CB  . ASP B 1 250 ? -4.951  -6.971  52.480  1.00 24.08 ? 250 ASP B CB  1 
ATOM   4198 C  CG  . ASP B 1 250 ? -5.360  -5.911  53.538  1.00 39.92 ? 250 ASP B CG  1 
ATOM   4199 O  OD1 . ASP B 1 250 ? -6.469  -5.211  53.375  1.00 46.40 ? 250 ASP B OD1 1 
ATOM   4200 O  OD2 . ASP B 1 250 ? -4.595  -5.732  54.527  1.00 44.35 ? 250 ASP B OD2 1 
ATOM   4201 N  N   . ARG B 1 251 ? -3.059  -5.346  50.503  1.00 18.75 ? 251 ARG B N   1 
ATOM   4202 C  CA  . ARG B 1 251 ? -2.206  -4.182  50.202  1.00 17.01 ? 251 ARG B CA  1 
ATOM   4203 C  C   . ARG B 1 251 ? -2.715  -3.402  48.989  1.00 17.85 ? 251 ARG B C   1 
ATOM   4204 O  O   . ARG B 1 251 ? -2.581  -2.181  48.956  1.00 15.76 ? 251 ARG B O   1 
ATOM   4205 C  CB  . ARG B 1 251 ? -0.755  -4.594  49.952  1.00 17.82 ? 251 ARG B CB  1 
ATOM   4206 C  CG  . ARG B 1 251 ? -0.055  -5.076  51.221  1.00 26.37 ? 251 ARG B CG  1 
ATOM   4207 C  CD  . ARG B 1 251 ? 1.407   -5.452  50.972  1.00 27.29 ? 251 ARG B CD  1 
ATOM   4208 N  NE  . ARG B 1 251 ? 2.226   -4.299  50.954  1.00 29.82 ? 251 ARG B NE  1 
ATOM   4209 C  CZ  . ARG B 1 251 ? 3.476   -4.200  50.516  1.00 26.07 ? 251 ARG B CZ  1 
ATOM   4210 N  NH1 . ARG B 1 251 ? 3.957   -4.931  49.521  1.00 20.77 ? 251 ARG B NH1 1 
ATOM   4211 N  NH2 . ARG B 1 251 ? 4.235   -3.256  51.058  1.00 24.06 ? 251 ARG B NH2 1 
ATOM   4212 N  N   . LEU B 1 252 ? -3.287  -4.104  48.008  1.00 15.69 ? 252 LEU B N   1 
ATOM   4213 C  CA  . LEU B 1 252 ? -3.916  -3.406  46.897  1.00 13.99 ? 252 LEU B CA  1 
ATOM   4214 C  C   . LEU B 1 252 ? -5.116  -2.594  47.344  1.00 13.54 ? 252 LEU B C   1 
ATOM   4215 O  O   . LEU B 1 252 ? -5.290  -1.444  46.922  1.00 14.08 ? 252 LEU B O   1 
ATOM   4216 C  CB  . LEU B 1 252 ? -4.279  -4.392  45.788  1.00 14.58 ? 252 LEU B CB  1 
ATOM   4217 C  CG  . LEU B 1 252 ? -3.099  -5.051  45.069  1.00 15.98 ? 252 LEU B CG  1 
ATOM   4218 C  CD1 . LEU B 1 252 ? -3.642  -6.244  44.280  1.00 20.00 ? 252 LEU B CD1 1 
ATOM   4219 C  CD2 . LEU B 1 252 ? -2.316  -4.061  44.140  1.00 17.96 ? 252 LEU B CD2 1 
ATOM   4220 N  N   . ASP B 1 253 ? -5.954  -3.176  48.205  1.00 15.14 ? 253 ASP B N   1 
ATOM   4221 C  CA  . ASP B 1 253 ? -7.080  -2.437  48.759  1.00 17.28 ? 253 ASP B CA  1 
ATOM   4222 C  C   . ASP B 1 253 ? -6.627  -1.210  49.548  1.00 17.67 ? 253 ASP B C   1 
ATOM   4223 O  O   . ASP B 1 253 ? -7.295  -0.176  49.499  1.00 19.96 ? 253 ASP B O   1 
ATOM   4224 C  CB  . ASP B 1 253 ? -7.992  -3.332  49.591  1.00 18.11 ? 253 ASP B CB  1 
ATOM   4225 C  CG  . ASP B 1 253 ? -8.772  -4.332  48.761  1.00 22.80 ? 253 ASP B CG  1 
ATOM   4226 O  OD1 . ASP B 1 253 ? -8.975  -4.076  47.588  1.00 23.38 ? 253 ASP B OD1 1 
ATOM   4227 O  OD2 . ASP B 1 253 ? -9.166  -5.381  49.317  1.00 27.98 ? 253 ASP B OD2 1 
ATOM   4228 N  N   . ARG B 1 254 ? -5.553  -1.367  50.323  1.00 17.59 ? 254 ARG B N   1 
ATOM   4229 C  CA  . ARG B 1 254 ? -5.076  -0.308  51.198  1.00 15.64 ? 254 ARG B CA  1 
ATOM   4230 C  C   . ARG B 1 254 ? -4.430  0.806   50.396  1.00 16.57 ? 254 ARG B C   1 
ATOM   4231 O  O   . ARG B 1 254 ? -4.640  1.973   50.697  1.00 16.86 ? 254 ARG B O   1 
ATOM   4232 C  CB  . ARG B 1 254 ? -4.134  -0.898  52.257  1.00 20.61 ? 254 ARG B CB  1 
ATOM   4233 C  CG  . ARG B 1 254 ? -3.761  0.096   53.352  1.00 29.43 ? 254 ARG B CG  1 
ATOM   4234 C  CD  . ARG B 1 254 ? -2.983  -0.527  54.504  1.00 38.56 ? 254 ARG B CD  1 
ATOM   4235 N  NE  . ARG B 1 254 ? -3.844  -1.341  55.369  1.00 48.19 ? 254 ARG B NE  1 
ATOM   4236 C  CZ  . ARG B 1 254 ? -3.826  -2.669  55.423  1.00 51.97 ? 254 ARG B CZ  1 
ATOM   4237 N  NH1 . ARG B 1 254 ? -3.313  -3.365  54.423  1.00 54.41 ? 254 ARG B NH1 1 
ATOM   4238 N  NH2 . ARG B 1 254 ? -4.359  -3.293  56.465  1.00 58.68 ? 254 ARG B NH2 1 
ATOM   4239 N  N   . PHE B 1 255 ? -3.653  0.458   49.364  1.00 14.68 ? 255 PHE B N   1 
ATOM   4240 C  CA  . PHE B 1 255 ? -2.762  1.444   48.771  1.00 14.88 ? 255 PHE B CA  1 
ATOM   4241 C  C   . PHE B 1 255 ? -2.933  1.721   47.293  1.00 13.75 ? 255 PHE B C   1 
ATOM   4242 O  O   . PHE B 1 255 ? -2.394  2.743   46.776  1.00 13.75 ? 255 PHE B O   1 
ATOM   4243 C  CB  . PHE B 1 255 ? -1.324  0.980   48.893  1.00 15.40 ? 255 PHE B CB  1 
ATOM   4244 C  CG  . PHE B 1 255 ? -0.869  0.873   50.317  1.00 15.71 ? 255 PHE B CG  1 
ATOM   4245 C  CD1 . PHE B 1 255 ? -0.710  2.028   51.053  1.00 19.69 ? 255 PHE B CD1 1 
ATOM   4246 C  CD2 . PHE B 1 255 ? -0.474  -0.322  50.882  1.00 18.71 ? 255 PHE B CD2 1 
ATOM   4247 C  CE1 . PHE B 1 255 ? -0.239  1.979   52.356  1.00 20.23 ? 255 PHE B CE1 1 
ATOM   4248 C  CE2 . PHE B 1 255 ? 0.081   -0.367  52.162  1.00 19.74 ? 255 PHE B CE2 1 
ATOM   4249 C  CZ  . PHE B 1 255 ? 0.222   0.793   52.890  1.00 21.42 ? 255 PHE B CZ  1 
ATOM   4250 N  N   . VAL B 1 256 ? -3.761  0.938   46.621  1.00 13.31 ? 256 VAL B N   1 
ATOM   4251 C  CA  . VAL B 1 256 ? -3.864  1.060   45.178  1.00 12.96 ? 256 VAL B CA  1 
ATOM   4252 C  C   . VAL B 1 256 ? -5.268  1.409   44.721  1.00 13.32 ? 256 VAL B C   1 
ATOM   4253 O  O   . VAL B 1 256 ? -5.424  2.331   43.907  1.00 15.39 ? 256 VAL B O   1 
ATOM   4254 C  CB  . VAL B 1 256 ? -3.301  -0.197  44.513  1.00 14.35 ? 256 VAL B CB  1 
ATOM   4255 C  CG1 . VAL B 1 256 ? -3.502  -0.148  43.008  1.00 15.39 ? 256 VAL B CG1 1 
ATOM   4256 C  CG2 . VAL B 1 256 ? -1.834  -0.403  44.869  1.00 15.82 ? 256 VAL B CG2 1 
ATOM   4257 N  N   . TRP B 1 257 ? -6.290  0.628   45.122  1.00 13.15 ? 257 TRP B N   1 
ATOM   4258 C  CA  . TRP B 1 257 ? -7.645  0.837   44.618  1.00 13.42 ? 257 TRP B CA  1 
ATOM   4259 C  C   . TRP B 1 257 ? -8.357  1.978   45.350  1.00 15.94 ? 257 TRP B C   1 
ATOM   4260 O  O   . TRP B 1 257 ? -8.378  2.048   46.583  1.00 14.84 ? 257 TRP B O   1 
ATOM   4261 C  CB  . TRP B 1 257 ? -8.514  -0.431  44.692  1.00 13.12 ? 257 TRP B CB  1 
ATOM   4262 C  CG  . TRP B 1 257 ? -7.886  -1.664  44.082  1.00 15.32 ? 257 TRP B CG  1 
ATOM   4263 C  CD1 . TRP B 1 257 ? -7.713  -2.906  44.658  1.00 15.15 ? 257 TRP B CD1 1 
ATOM   4264 C  CD2 . TRP B 1 257 ? -7.440  -1.792  42.712  1.00 15.03 ? 257 TRP B CD2 1 
ATOM   4265 N  NE1 . TRP B 1 257 ? -7.145  -3.759  43.748  1.00 16.91 ? 257 TRP B NE1 1 
ATOM   4266 C  CE2 . TRP B 1 257 ? -6.963  -3.112  42.542  1.00 17.71 ? 257 TRP B CE2 1 
ATOM   4267 C  CE3 . TRP B 1 257 ? -7.471  -0.927  41.604  1.00 17.96 ? 257 TRP B CE3 1 
ATOM   4268 C  CZ2 . TRP B 1 257 ? -6.472  -3.559  41.307  1.00 16.22 ? 257 TRP B CZ2 1 
ATOM   4269 C  CZ3 . TRP B 1 257 ? -6.902  -1.354  40.400  1.00 15.53 ? 257 TRP B CZ3 1 
ATOM   4270 C  CH2 . TRP B 1 257 ? -6.456  -2.653  40.260  1.00 16.42 ? 257 TRP B CH2 1 
ATOM   4271 N  N   . ALA B 1 258 ? -9.085  2.774   44.552  1.00 15.31 ? 258 ALA B N   1 
ATOM   4272 C  CA  . ALA B 1 258 ? -9.964  3.783   45.088  1.00 14.89 ? 258 ALA B CA  1 
ATOM   4273 C  C   . ALA B 1 258 ? -11.212 3.096   45.709  1.00 16.43 ? 258 ALA B C   1 
ATOM   4274 O  O   . ALA B 1 258 ? -11.765 2.141   45.174  1.00 15.10 ? 258 ALA B O   1 
ATOM   4275 C  CB  . ALA B 1 258 ? -10.371 4.721   43.992  1.00 16.22 ? 258 ALA B CB  1 
ATOM   4276 N  N   . ALA B 1 259 ? -11.638 3.560   46.898  1.00 20.79 ? 259 ALA B N   1 
ATOM   4277 C  CA  . ALA B 1 259 ? -12.792 2.995   47.605  1.00 21.91 ? 259 ALA B CA  1 
ATOM   4278 C  C   . ALA B 1 259 ? -13.963 3.993   47.500  1.00 23.20 ? 259 ALA B C   1 
ATOM   4279 O  O   . ALA B 1 259 ? -13.741 5.198   47.334  1.00 22.15 ? 259 ALA B O   1 
ATOM   4280 C  CB  . ALA B 1 259 ? -12.399 2.763   49.039  1.00 22.58 ? 259 ALA B CB  1 
ATOM   4281 N  N   . GLU B 1 260 ? -15.213 3.520   47.667  1.00 26.82 ? 260 GLU B N   1 
ATOM   4282 C  CA  . GLU B 1 260 ? -16.348 4.444   47.578  1.00 30.80 ? 260 GLU B CA  1 
ATOM   4283 C  C   . GLU B 1 260 ? -16.210 5.564   48.617  1.00 28.00 ? 260 GLU B C   1 
ATOM   4284 O  O   . GLU B 1 260 ? -16.470 6.728   48.333  1.00 31.24 ? 260 GLU B O   1 
ATOM   4285 C  CB  . GLU B 1 260 ? -17.680 3.722   47.827  1.00 35.16 ? 260 GLU B CB  1 
ATOM   4286 C  CG  . GLU B 1 260 ? -18.890 4.607   47.576  1.00 33.88 ? 260 GLU B CG  1 
ATOM   4287 N  N   . LYS B 1 261 ? -15.709 5.211   49.801  1.00 26.27 ? 261 LYS B N   1 
ATOM   4288 C  CA  . LYS B 1 261 ? -15.687 6.137   50.930  1.00 34.96 ? 261 LYS B CA  1 
ATOM   4289 C  C   . LYS B 1 261 ? -14.648 7.228   50.705  1.00 32.16 ? 261 LYS B C   1 
ATOM   4290 O  O   . LYS B 1 261 ? -14.666 8.203   51.432  1.00 27.30 ? 261 LYS B O   1 
ATOM   4291 C  CB  . LYS B 1 261 ? -15.442 5.454   52.297  1.00 39.57 ? 261 LYS B CB  1 
ATOM   4292 C  CG  . LYS B 1 261 ? -14.033 4.905   52.564  1.00 43.52 ? 261 LYS B CG  1 
ATOM   4293 C  CD  . LYS B 1 261 ? -13.836 4.114   53.879  1.00 43.89 ? 261 LYS B CD  1 
ATOM   4294 N  N   . ASP B 1 262 ? -13.821 7.120   49.645  1.00 22.15 ? 262 ASP B N   1 
ATOM   4295 C  CA  . ASP B 1 262 ? -12.742 8.051   49.473  1.00 20.12 ? 262 ASP B CA  1 
ATOM   4296 C  C   . ASP B 1 262 ? -13.261 9.352   48.913  1.00 20.80 ? 262 ASP B C   1 
ATOM   4297 O  O   . ASP B 1 262 ? -12.577 10.370  49.009  1.00 26.00 ? 262 ASP B O   1 
ATOM   4298 C  CB  . ASP B 1 262 ? -11.642 7.513   48.545  1.00 20.52 ? 262 ASP B CB  1 
ATOM   4299 C  CG  . ASP B 1 262 ? -10.853 6.354   49.071  1.00 25.78 ? 262 ASP B CG  1 
ATOM   4300 O  OD1 . ASP B 1 262 ? -10.997 6.041   50.261  1.00 23.18 ? 262 ASP B OD1 1 
ATOM   4301 O  OD2 . ASP B 1 262 ? -10.158 5.738   48.272  1.00 20.75 ? 262 ASP B OD2 1 
ATOM   4302 N  N   . GLY B 1 263 ? -14.485 9.350   48.378  1.00 23.26 ? 263 GLY B N   1 
ATOM   4303 C  CA  . GLY B 1 263 ? -15.044 10.652  48.077  1.00 24.39 ? 263 GLY B CA  1 
ATOM   4304 C  C   . GLY B 1 263 ? -15.524 10.799  46.652  1.00 27.85 ? 263 GLY B C   1 
ATOM   4305 O  O   . GLY B 1 263 ? -16.306 11.730  46.382  1.00 27.86 ? 263 GLY B O   1 
ATOM   4306 N  N   . THR B 1 264 ? -15.126 9.875   45.745  1.00 22.45 ? 264 THR B N   1 
ATOM   4307 C  CA  . THR B 1 264 ? -15.578 9.996   44.358  1.00 21.95 ? 264 THR B CA  1 
ATOM   4308 C  C   . THR B 1 264 ? -16.141 8.649   43.931  1.00 21.06 ? 264 THR B C   1 
ATOM   4309 O  O   . THR B 1 264 ? -15.394 7.698   43.631  1.00 18.42 ? 264 THR B O   1 
ATOM   4310 C  CB  . THR B 1 264 ? -14.431 10.379  43.405  1.00 24.16 ? 264 THR B CB  1 
ATOM   4311 O  OG1 . THR B 1 264 ? -13.780 11.546  43.910  1.00 20.91 ? 264 THR B OG1 1 
ATOM   4312 C  CG2 . THR B 1 264 ? -14.925 10.583  41.991  1.00 22.65 ? 264 THR B CG2 1 
ATOM   4313 N  N   . PRO B 1 265 ? -17.472 8.504   44.021  1.00 22.24 ? 265 PRO B N   1 
ATOM   4314 C  CA  . PRO B 1 265 ? -18.105 7.207   43.734  1.00 19.73 ? 265 PRO B CA  1 
ATOM   4315 C  C   . PRO B 1 265 ? -17.806 6.592   42.354  1.00 20.51 ? 265 PRO B C   1 
ATOM   4316 O  O   . PRO B 1 265 ? -17.664 5.354   42.249  1.00 19.07 ? 265 PRO B O   1 
ATOM   4317 C  CB  . PRO B 1 265 ? -19.596 7.552   43.904  1.00 25.30 ? 265 PRO B CB  1 
ATOM   4318 C  CG  . PRO B 1 265 ? -19.612 8.646   44.962  1.00 23.98 ? 265 PRO B CG  1 
ATOM   4319 C  CD  . PRO B 1 265 ? -18.409 9.507   44.605  1.00 22.57 ? 265 PRO B CD  1 
ATOM   4320 N  N   . TRP B 1 266 ? -17.709 7.410   41.286  1.00 17.59 ? 266 TRP B N   1 
ATOM   4321 C  CA  . TRP B 1 266 ? -17.517 6.830   39.953  1.00 16.84 ? 266 TRP B CA  1 
ATOM   4322 C  C   . TRP B 1 266 ? -16.149 6.146   39.861  1.00 14.95 ? 266 TRP B C   1 
ATOM   4323 O  O   . TRP B 1 266 ? -15.933 5.316   38.970  1.00 17.03 ? 266 TRP B O   1 
ATOM   4324 C  CB  . TRP B 1 266 ? -17.748 7.872   38.828  1.00 16.60 ? 266 TRP B CB  1 
ATOM   4325 C  CG  . TRP B 1 266 ? -16.700 8.952   38.673  1.00 17.95 ? 266 TRP B CG  1 
ATOM   4326 C  CD1 . TRP B 1 266 ? -16.729 10.231  39.171  1.00 17.39 ? 266 TRP B CD1 1 
ATOM   4327 C  CD2 . TRP B 1 266 ? -15.452 8.847   37.983  1.00 16.34 ? 266 TRP B CD2 1 
ATOM   4328 N  NE1 . TRP B 1 266 ? -15.605 10.949  38.794  1.00 17.11 ? 266 TRP B NE1 1 
ATOM   4329 C  CE2 . TRP B 1 266 ? -14.804 10.123  38.051  1.00 17.94 ? 266 TRP B CE2 1 
ATOM   4330 C  CE3 . TRP B 1 266 ? -14.857 7.853   37.186  1.00 18.13 ? 266 TRP B CE3 1 
ATOM   4331 C  CZ2 . TRP B 1 266 ? -13.597 10.383  37.427  1.00 19.00 ? 266 TRP B CZ2 1 
ATOM   4332 C  CZ3 . TRP B 1 266 ? -13.675 8.135   36.566  1.00 17.79 ? 266 TRP B CZ3 1 
ATOM   4333 C  CH2 . TRP B 1 266 ? -12.992 9.342   36.780  1.00 17.62 ? 266 TRP B CH2 1 
ATOM   4334 N  N   . MET B 1 267 ? -15.211 6.497   40.746  1.00 13.78 ? 267 MET B N   1 
ATOM   4335 C  CA  . MET B 1 267 ? -13.852 5.982   40.669  1.00 14.76 ? 267 MET B CA  1 
ATOM   4336 C  C   . MET B 1 267 ? -13.687 4.703   41.491  1.00 16.86 ? 267 MET B C   1 
ATOM   4337 O  O   . MET B 1 267 ? -12.576 4.201   41.546  1.00 14.68 ? 267 MET B O   1 
ATOM   4338 C  CB  . MET B 1 267 ? -12.826 7.001   41.138  1.00 13.15 ? 267 MET B CB  1 
ATOM   4339 C  CG  . MET B 1 267 ? -12.293 7.894   40.048  1.00 13.63 ? 267 MET B CG  1 
ATOM   4340 S  SD  . MET B 1 267 ? -11.337 6.946   38.836  1.00 14.74 ? 267 MET B SD  1 
ATOM   4341 C  CE  . MET B 1 267 ? -9.967  6.422   39.841  1.00 16.56 ? 267 MET B CE  1 
ATOM   4342 N  N   . THR B 1 268 ? -14.721 4.214   42.216  1.00 16.90 ? 268 THR B N   1 
ATOM   4343 C  CA  . THR B 1 268 ? -14.548 3.060   43.077  1.00 14.85 ? 268 THR B CA  1 
ATOM   4344 C  C   . THR B 1 268 ? -14.018 1.864   42.257  1.00 15.47 ? 268 THR B C   1 
ATOM   4345 O  O   . THR B 1 268 ? -14.633 1.494   41.286  1.00 14.80 ? 268 THR B O   1 
ATOM   4346 C  CB  . THR B 1 268 ? -15.908 2.672   43.691  1.00 18.30 ? 268 THR B CB  1 
ATOM   4347 O  OG1 . THR B 1 268 ? -16.342 3.826   44.415  1.00 18.62 ? 268 THR B OG1 1 
ATOM   4348 C  CG2 . THR B 1 268 ? -15.831 1.431   44.548  1.00 22.24 ? 268 THR B CG2 1 
ATOM   4349 N  N   . GLY B 1 269 ? -12.913 1.259   42.663  1.00 15.11 ? 269 GLY B N   1 
ATOM   4350 C  CA  . GLY B 1 269 ? -12.258 0.179   41.955  1.00 13.64 ? 269 GLY B CA  1 
ATOM   4351 C  C   . GLY B 1 269 ? -11.267 0.613   40.880  1.00 14.41 ? 269 GLY B C   1 
ATOM   4352 O  O   . GLY B 1 269 ? -10.611 -0.227  40.298  1.00 14.74 ? 269 GLY B O   1 
ATOM   4353 N  N   . GLY B 1 270 ? -11.178 1.912   40.619  1.00 13.58 ? 270 GLY B N   1 
ATOM   4354 C  CA  . GLY B 1 270 ? -10.140 2.525   39.814  1.00 13.21 ? 270 GLY B CA  1 
ATOM   4355 C  C   . GLY B 1 270 ? -8.891  2.788   40.633  1.00 12.68 ? 270 GLY B C   1 
ATOM   4356 O  O   . GLY B 1 270 ? -8.748  2.349   41.792  1.00 12.16 ? 270 GLY B O   1 
ATOM   4357 N  N   . SER B 1 271 ? -7.942  3.482   40.004  1.00 10.80 ? 271 SER B N   1 
ATOM   4358 C  CA  . SER B 1 271 ? -6.724  3.843   40.692  1.00 11.44 ? 271 SER B CA  1 
ATOM   4359 C  C   . SER B 1 271 ? -6.230  5.154   40.067  1.00 11.57 ? 271 SER B C   1 
ATOM   4360 O  O   . SER B 1 271 ? -6.831  5.597   39.107  1.00 13.22 ? 271 SER B O   1 
ATOM   4361 C  CB  . SER B 1 271 ? -5.675  2.699   40.563  1.00 12.24 ? 271 SER B CB  1 
ATOM   4362 O  OG  . SER B 1 271 ? -4.576  2.916   41.386  1.00 11.69 ? 271 SER B OG  1 
ATOM   4363 N  N   . TYR B 1 272 ? -5.136  5.696   40.579  1.00 11.60 ? 272 TYR B N   1 
ATOM   4364 C  CA  . TYR B 1 272 ? -4.569  6.926   40.061  1.00 10.88 ? 272 TYR B CA  1 
ATOM   4365 C  C   . TYR B 1 272 ? -3.160  6.592   39.603  1.00 12.15 ? 272 TYR B C   1 
ATOM   4366 O  O   . TYR B 1 272 ? -2.429  5.929   40.336  1.00 14.26 ? 272 TYR B O   1 
ATOM   4367 C  CB  . TYR B 1 272 ? -4.610  8.058   41.121  1.00 12.72 ? 272 TYR B CB  1 
ATOM   4368 C  CG  . TYR B 1 272 ? -6.002  8.412   41.522  1.00 11.74 ? 272 TYR B CG  1 
ATOM   4369 C  CD1 . TYR B 1 272 ? -6.769  9.258   40.757  1.00 11.59 ? 272 TYR B CD1 1 
ATOM   4370 C  CD2 . TYR B 1 272 ? -6.665  7.688   42.496  1.00 13.52 ? 272 TYR B CD2 1 
ATOM   4371 C  CE1 . TYR B 1 272 ? -8.074  9.543   41.088  1.00 11.81 ? 272 TYR B CE1 1 
ATOM   4372 C  CE2 . TYR B 1 272 ? -7.990  7.937   42.845  1.00 13.23 ? 272 TYR B CE2 1 
ATOM   4373 C  CZ  . TYR B 1 272 ? -8.693  8.898   42.141  1.00 12.29 ? 272 TYR B CZ  1 
ATOM   4374 O  OH  . TYR B 1 272 ? -10.016 9.130   42.412  1.00 16.08 ? 272 TYR B OH  1 
ATOM   4375 N  N   . LEU B 1 273 ? -2.802  7.139   38.439  1.00 10.95 ? 273 LEU B N   1 
ATOM   4376 C  CA  . LEU B 1 273 ? -1.537  6.847   37.787  1.00 10.67 ? 273 LEU B CA  1 
ATOM   4377 C  C   . LEU B 1 273 ? -0.721  8.112   37.700  1.00 11.22 ? 273 LEU B C   1 
ATOM   4378 O  O   . LEU B 1 273 ? -1.202  9.144   37.211  1.00 11.77 ? 273 LEU B O   1 
ATOM   4379 C  CB  . LEU B 1 273 ? -1.855  6.288   36.417  1.00 11.72 ? 273 LEU B CB  1 
ATOM   4380 C  CG  . LEU B 1 273 ? -0.651  6.050   35.523  1.00 12.52 ? 273 LEU B CG  1 
ATOM   4381 C  CD1 . LEU B 1 273 ? 0.325   5.030   36.158  1.00 12.23 ? 273 LEU B CD1 1 
ATOM   4382 C  CD2 . LEU B 1 273 ? -1.142  5.545   34.174  1.00 13.01 ? 273 LEU B CD2 1 
ATOM   4383 N  N   . VAL B 1 274 ? 0.551   7.978   38.076  1.00 10.79 ? 274 VAL B N   1 
ATOM   4384 C  CA  . VAL B 1 274 ? 1.570   8.977   37.798  1.00 10.25 ? 274 VAL B CA  1 
ATOM   4385 C  C   . VAL B 1 274 ? 2.563   8.401   36.822  1.00 11.17 ? 274 VAL B C   1 
ATOM   4386 O  O   . VAL B 1 274 ? 3.044   7.304   37.048  1.00 12.23 ? 274 VAL B O   1 
ATOM   4387 C  CB  . VAL B 1 274 ? 2.238   9.438   39.097  1.00 11.36 ? 274 VAL B CB  1 
ATOM   4388 C  CG1 . VAL B 1 274 ? 3.434   10.321  38.747  1.00 12.36 ? 274 VAL B CG1 1 
ATOM   4389 C  CG2 . VAL B 1 274 ? 1.262   10.198  39.980  1.00 11.00 ? 274 VAL B CG2 1 
ATOM   4390 N  N   . ALA B 1 275 ? 2.786   9.129   35.712  1.00 9.93  ? 275 ALA B N   1 
ATOM   4391 C  CA  . ALA B 1 275 ? 3.788   8.765   34.726  1.00 11.52 ? 275 ALA B CA  1 
ATOM   4392 C  C   . ALA B 1 275 ? 4.891   9.826   34.753  1.00 12.16 ? 275 ALA B C   1 
ATOM   4393 O  O   . ALA B 1 275 ? 4.606   11.023  34.781  1.00 13.62 ? 275 ALA B O   1 
ATOM   4394 C  CB  . ALA B 1 275 ? 3.182   8.759   33.348  1.00 12.15 ? 275 ALA B CB  1 
ATOM   4395 N  N   . ARG B 1 276 ? 6.123   9.368   34.874  1.00 11.06 ? 276 ARG B N   1 
ATOM   4396 C  CA  . ARG B 1 276 ? 7.288   10.257  34.793  1.00 12.40 ? 276 ARG B CA  1 
ATOM   4397 C  C   . ARG B 1 276 ? 8.279   9.639   33.838  1.00 11.85 ? 276 ARG B C   1 
ATOM   4398 O  O   . ARG B 1 276 ? 8.737   8.528   34.034  1.00 12.64 ? 276 ARG B O   1 
ATOM   4399 C  CB  . ARG B 1 276 ? 7.959   10.503  36.150  1.00 12.38 ? 276 ARG B CB  1 
ATOM   4400 C  CG  . ARG B 1 276 ? 7.025   10.985  37.248  1.00 12.44 ? 276 ARG B CG  1 
ATOM   4401 C  CD  . ARG B 1 276 ? 6.663   12.450  37.094  1.00 12.11 ? 276 ARG B CD  1 
ATOM   4402 N  NE  . ARG B 1 276 ? 7.809   13.290  37.522  1.00 14.66 ? 276 ARG B NE  1 
ATOM   4403 C  CZ  . ARG B 1 276 ? 7.695   14.543  38.001  1.00 14.74 ? 276 ARG B CZ  1 
ATOM   4404 N  NH1 . ARG B 1 276 ? 6.578   15.261  37.842  1.00 13.47 ? 276 ARG B NH1 1 
ATOM   4405 N  NH2 . ARG B 1 276 ? 8.804   15.114  38.451  1.00 14.02 ? 276 ARG B NH2 1 
ATOM   4406 N  N   . ARG B 1 277 ? 8.686   10.444  32.854  1.00 13.16 ? 277 ARG B N   1 
ATOM   4407 C  CA  . ARG B 1 277 ? 9.742   10.065  31.951  1.00 14.27 ? 277 ARG B CA  1 
ATOM   4408 C  C   . ARG B 1 277 ? 11.025  10.557  32.596  1.00 13.16 ? 277 ARG B C   1 
ATOM   4409 O  O   . ARG B 1 277 ? 11.170  11.754  32.756  1.00 14.27 ? 277 ARG B O   1 
ATOM   4410 C  CB  . ARG B 1 277 ? 9.523   10.681  30.558  1.00 15.49 ? 277 ARG B CB  1 
ATOM   4411 C  CG  . ARG B 1 277 ? 10.454  10.023  29.530  1.00 19.12 ? 277 ARG B CG  1 
ATOM   4412 C  CD  . ARG B 1 277 ? 10.153  10.625  28.158  1.00 21.69 ? 277 ARG B CD  1 
ATOM   4413 N  NE  . ARG B 1 277 ? 10.992  10.019  27.145  1.00 22.21 ? 277 ARG B NE  1 
ATOM   4414 C  CZ  . ARG B 1 277 ? 12.140  10.515  26.728  1.00 27.57 ? 277 ARG B CZ  1 
ATOM   4415 N  NH1 . ARG B 1 277 ? 12.619  11.615  27.294  1.00 30.87 ? 277 ARG B NH1 1 
ATOM   4416 N  NH2 . ARG B 1 277 ? 12.803  9.915   25.741  1.00 28.28 ? 277 ARG B NH2 1 
ATOM   4417 N  N   . ILE B 1 278 ? 11.892  9.616   32.981  1.00 13.08 ? 278 ILE B N   1 
ATOM   4418 C  CA  . ILE B 1 278 ? 13.039  9.965   33.755  1.00 12.65 ? 278 ILE B CA  1 
ATOM   4419 C  C   . ILE B 1 278 ? 14.252  9.560   32.918  1.00 13.84 ? 278 ILE B C   1 
ATOM   4420 O  O   . ILE B 1 278 ? 14.552  8.360   32.802  1.00 16.01 ? 278 ILE B O   1 
ATOM   4421 C  CB  . ILE B 1 278 ? 13.024  9.292   35.132  1.00 12.55 ? 278 ILE B CB  1 
ATOM   4422 C  CG1 . ILE B 1 278 ? 11.724  9.456   35.905  1.00 12.60 ? 278 ILE B CG1 1 
ATOM   4423 C  CG2 . ILE B 1 278 ? 14.272  9.761   35.860  1.00 15.17 ? 278 ILE B CG2 1 
ATOM   4424 C  CD1 . ILE B 1 278 ? 11.677  8.755   37.237  1.00 14.11 ? 278 ILE B CD1 1 
ATOM   4425 N  N   . ARG B 1 279 ? 14.952  10.565  32.398  1.00 12.87 ? 279 ARG B N   1 
ATOM   4426 C  CA  . ARG B 1 279 ? 16.196  10.326  31.677  1.00 16.32 ? 279 ARG B CA  1 
ATOM   4427 C  C   . ARG B 1 279 ? 17.294  9.982   32.687  1.00 14.20 ? 279 ARG B C   1 
ATOM   4428 O  O   . ARG B 1 279 ? 17.400  10.549  33.751  1.00 16.85 ? 279 ARG B O   1 
ATOM   4429 C  CB  . ARG B 1 279 ? 16.481  11.576  30.850  1.00 19.32 ? 279 ARG B CB  1 
ATOM   4430 C  CG  . ARG B 1 279 ? 17.848  11.649  30.229  1.00 29.56 ? 279 ARG B CG  1 
ATOM   4431 C  CD  . ARG B 1 279 ? 17.983  10.634  29.110  1.00 32.04 ? 279 ARG B CD  1 
ATOM   4432 N  NE  . ARG B 1 279 ? 19.345  10.667  28.552  1.00 38.81 ? 279 ARG B NE  1 
ATOM   4433 C  CZ  . ARG B 1 279 ? 19.773  11.672  27.779  1.00 44.93 ? 279 ARG B CZ  1 
ATOM   4434 N  NH1 . ARG B 1 279 ? 18.892  12.425  27.149  1.00 36.00 ? 279 ARG B NH1 1 
ATOM   4435 N  NH2 . ARG B 1 279 ? 21.067  11.916  27.622  1.00 61.00 ? 279 ARG B NH2 1 
ATOM   4436 N  N   . MET B 1 280 ? 18.171  9.060   32.281  1.00 13.91 ? 280 MET B N   1 
ATOM   4437 C  CA  . MET B 1 280 ? 19.379  8.747   33.035  1.00 13.79 ? 280 MET B CA  1 
ATOM   4438 C  C   . MET B 1 280 ? 20.567  9.356   32.288  1.00 15.97 ? 280 MET B C   1 
ATOM   4439 O  O   . MET B 1 280 ? 20.673  9.242   31.061  1.00 13.74 ? 280 MET B O   1 
ATOM   4440 C  CB  . MET B 1 280 ? 19.551  7.236   33.120  1.00 15.47 ? 280 MET B CB  1 
ATOM   4441 C  CG  . MET B 1 280 ? 18.545  6.598   33.985  1.00 15.93 ? 280 MET B CG  1 
ATOM   4442 S  SD  . MET B 1 280 ? 18.553  4.797   33.696  1.00 16.56 ? 280 MET B SD  1 
ATOM   4443 C  CE  . MET B 1 280 ? 17.355  4.292   34.933  1.00 18.81 ? 280 MET B CE  1 
ATOM   4444 N  N   . HIS B 1 281 ? 21.488  9.921   33.059  1.00 15.91 ? 281 HIS B N   1 
ATOM   4445 C  CA  . HIS B 1 281 ? 22.754  10.377  32.529  1.00 14.71 ? 281 HIS B CA  1 
ATOM   4446 C  C   . HIS B 1 281 ? 23.715  9.196   32.552  1.00 13.80 ? 281 HIS B C   1 
ATOM   4447 O  O   . HIS B 1 281 ? 24.508  8.996   33.481  1.00 14.78 ? 281 HIS B O   1 
ATOM   4448 C  CB  . HIS B 1 281 ? 23.252  11.524  33.390  1.00 17.48 ? 281 HIS B CB  1 
ATOM   4449 C  CG  . HIS B 1 281 ? 22.355  12.712  33.428  1.00 20.44 ? 281 HIS B CG  1 
ATOM   4450 N  ND1 . HIS B 1 281 ? 21.810  13.306  32.292  1.00 25.05 ? 281 HIS B ND1 1 
ATOM   4451 C  CD2 . HIS B 1 281 ? 21.903  13.381  34.529  1.00 27.15 ? 281 HIS B CD2 1 
ATOM   4452 C  CE1 . HIS B 1 281 ? 21.015  14.313  32.695  1.00 28.93 ? 281 HIS B CE1 1 
ATOM   4453 N  NE2 . HIS B 1 281 ? 21.075  14.377  34.076  1.00 24.25 ? 281 HIS B NE2 1 
ATOM   4454 N  N   . ILE B 1 282 ? 23.522  8.320   31.574  1.00 15.13 ? 282 ILE B N   1 
ATOM   4455 C  CA  . ILE B 1 282 ? 24.144  7.013   31.518  1.00 16.25 ? 282 ILE B CA  1 
ATOM   4456 C  C   . ILE B 1 282 ? 25.666  7.153   31.587  1.00 14.35 ? 282 ILE B C   1 
ATOM   4457 O  O   . ILE B 1 282 ? 26.347  6.457   32.340  1.00 18.20 ? 282 ILE B O   1 
ATOM   4458 C  CB  . ILE B 1 282 ? 23.707  6.342   30.201  1.00 20.04 ? 282 ILE B CB  1 
ATOM   4459 C  CG1 . ILE B 1 282 ? 22.229  5.970   30.168  1.00 22.61 ? 282 ILE B CG1 1 
ATOM   4460 C  CG2 . ILE B 1 282 ? 24.537  5.143   29.846  1.00 19.96 ? 282 ILE B CG2 1 
ATOM   4461 C  CD1 . ILE B 1 282 ? 21.815  4.945   31.147  1.00 25.52 ? 282 ILE B CD1 1 
ATOM   4462 N  N   . GLU B 1 283 ? 26.218  8.034   30.720  1.00 18.74 ? 283 GLU B N   1 
ATOM   4463 C  CA  . GLU B 1 283 ? 27.684  8.153   30.603  1.00 20.17 ? 283 GLU B CA  1 
ATOM   4464 C  C   . GLU B 1 283 ? 28.311  8.680   31.906  1.00 22.06 ? 283 GLU B C   1 
ATOM   4465 O  O   . GLU B 1 283 ? 29.432  8.238   32.255  1.00 22.56 ? 283 GLU B O   1 
ATOM   4466 C  CB  . GLU B 1 283 ? 28.089  8.963   29.353  1.00 20.55 ? 283 GLU B CB  1 
ATOM   4467 C  CG  . GLU B 1 283 ? 27.613  8.385   28.059  1.00 21.03 ? 283 GLU B CG  1 
ATOM   4468 C  CD  . GLU B 1 283 ? 26.118  8.642   27.746  1.00 23.12 ? 283 GLU B CD  1 
ATOM   4469 O  OE1 . GLU B 1 283 ? 25.452  9.390   28.492  1.00 21.25 ? 283 GLU B OE1 1 
ATOM   4470 O  OE2 . GLU B 1 283 ? 25.596  8.035   26.783  1.00 22.04 ? 283 GLU B OE2 1 
ATOM   4471 N  N   . THR B 1 284 ? 27.605  9.546   32.664  1.00 19.08 ? 284 THR B N   1 
ATOM   4472 C  CA  . THR B 1 284 ? 28.064  10.026  33.964  1.00 19.89 ? 284 THR B CA  1 
ATOM   4473 C  C   . THR B 1 284 ? 28.100  8.858   34.971  1.00 19.43 ? 284 THR B C   1 
ATOM   4474 O  O   . THR B 1 284 ? 29.051  8.630   35.745  1.00 16.69 ? 284 THR B O   1 
ATOM   4475 C  CB  . THR B 1 284 ? 27.178  11.213  34.411  1.00 24.34 ? 284 THR B CB  1 
ATOM   4476 O  OG1 . THR B 1 284 ? 27.337  12.285  33.470  1.00 28.24 ? 284 THR B OG1 1 
ATOM   4477 C  CG2 . THR B 1 284 ? 27.548  11.770  35.775  1.00 29.13 ? 284 THR B CG2 1 
ATOM   4478 N  N   . TRP B 1 285 ? 26.959  8.179   35.044  1.00 15.28 ? 285 TRP B N   1 
ATOM   4479 C  CA  . TRP B 1 285 ? 26.805  7.051   35.925  1.00 14.82 ? 285 TRP B CA  1 
ATOM   4480 C  C   . TRP B 1 285 ? 27.901  6.006   35.713  1.00 13.91 ? 285 TRP B C   1 
ATOM   4481 O  O   . TRP B 1 285 ? 28.391  5.439   36.686  1.00 15.90 ? 285 TRP B O   1 
ATOM   4482 C  CB  . TRP B 1 285 ? 25.413  6.462   35.714  1.00 14.07 ? 285 TRP B CB  1 
ATOM   4483 C  CG  . TRP B 1 285 ? 25.169  5.181   36.479  1.00 13.90 ? 285 TRP B CG  1 
ATOM   4484 C  CD1 . TRP B 1 285 ? 25.122  3.914   35.991  1.00 13.55 ? 285 TRP B CD1 1 
ATOM   4485 C  CD2 . TRP B 1 285 ? 24.803  5.082   37.845  1.00 13.33 ? 285 TRP B CD2 1 
ATOM   4486 N  NE1 . TRP B 1 285 ? 24.860  3.025   36.982  1.00 13.85 ? 285 TRP B NE1 1 
ATOM   4487 C  CE2 . TRP B 1 285 ? 24.645  3.711   38.139  1.00 16.32 ? 285 TRP B CE2 1 
ATOM   4488 C  CE3 . TRP B 1 285 ? 24.661  6.010   38.882  1.00 15.69 ? 285 TRP B CE3 1 
ATOM   4489 C  CZ2 . TRP B 1 285 ? 24.273  3.256   39.404  1.00 15.66 ? 285 TRP B CZ2 1 
ATOM   4490 C  CZ3 . TRP B 1 285 ? 24.293  5.555   40.140  1.00 19.06 ? 285 TRP B CZ3 1 
ATOM   4491 C  CH2 . TRP B 1 285 ? 24.106  4.205   40.398  1.00 16.21 ? 285 TRP B CH2 1 
ATOM   4492 N  N   . ASP B 1 286 ? 28.182  5.677   34.434  1.00 14.64 ? 286 ASP B N   1 
ATOM   4493 C  CA  . ASP B 1 286 ? 29.093  4.611   34.102  1.00 17.58 ? 286 ASP B CA  1 
ATOM   4494 C  C   . ASP B 1 286 ? 30.535  4.990   34.519  1.00 18.14 ? 286 ASP B C   1 
ATOM   4495 O  O   . ASP B 1 286 ? 31.374  4.121   34.609  1.00 20.36 ? 286 ASP B O   1 
ATOM   4496 C  CB  . ASP B 1 286 ? 28.995  4.223   32.625  1.00 16.86 ? 286 ASP B CB  1 
ATOM   4497 C  CG  . ASP B 1 286 ? 27.692  3.510   32.265  1.00 15.70 ? 286 ASP B CG  1 
ATOM   4498 O  OD1 . ASP B 1 286 ? 27.041  2.969   33.176  1.00 16.90 ? 286 ASP B OD1 1 
ATOM   4499 O  OD2 . ASP B 1 286 ? 27.368  3.482   31.016  1.00 16.79 ? 286 ASP B OD2 1 
ATOM   4500 N  N   . ARG B 1 287 ? 30.800  6.275   34.768  1.00 17.77 ? 287 ARG B N   1 
ATOM   4501 C  CA  . ARG B 1 287 ? 32.117  6.683   35.267  1.00 20.17 ? 287 ARG B CA  1 
ATOM   4502 C  C   . ARG B 1 287 ? 32.168  6.738   36.792  1.00 18.33 ? 287 ARG B C   1 
ATOM   4503 O  O   . ARG B 1 287 ? 33.266  6.921   37.361  1.00 22.29 ? 287 ARG B O   1 
ATOM   4504 C  CB  . ARG B 1 287 ? 32.488  8.094   34.765  1.00 25.49 ? 287 ARG B CB  1 
ATOM   4505 C  CG  . ARG B 1 287 ? 32.859  8.172   33.300  1.00 32.14 ? 287 ARG B CG  1 
ATOM   4506 C  CD  . ARG B 1 287 ? 33.255  9.598   32.930  1.00 37.86 ? 287 ARG B CD  1 
ATOM   4507 N  NE  . ARG B 1 287 ? 33.078  9.863   31.497  1.00 41.50 ? 287 ARG B NE  1 
ATOM   4508 N  N   . ALA B 1 288 ? 31.081  6.439   37.483  1.00 15.85 ? 288 ALA B N   1 
ATOM   4509 C  CA  . ALA B 1 288 ? 31.035  6.335   38.924  1.00 16.96 ? 288 ALA B CA  1 
ATOM   4510 C  C   . ALA B 1 288 ? 31.662  5.028   39.394  1.00 18.06 ? 288 ALA B C   1 
ATOM   4511 O  O   . ALA B 1 288 ? 31.538  3.964   38.792  1.00 18.88 ? 288 ALA B O   1 
ATOM   4512 C  CB  . ALA B 1 288 ? 29.602  6.494   39.471  1.00 20.45 ? 288 ALA B CB  1 
ATOM   4513 N  N   . SER B 1 289 ? 32.301  5.090   40.559  1.00 15.86 ? 289 SER B N   1 
ATOM   4514 C  CA  . SER B 1 289 ? 32.826  3.876   41.145  1.00 17.27 ? 289 SER B CA  1 
ATOM   4515 C  C   . SER B 1 289 ? 31.687  2.961   41.581  1.00 17.44 ? 289 SER B C   1 
ATOM   4516 O  O   . SER B 1 289 ? 30.569  3.404   41.893  1.00 19.05 ? 289 SER B O   1 
ATOM   4517 C  CB  . SER B 1 289 ? 33.755  4.209   42.304  1.00 15.97 ? 289 SER B CB  1 
ATOM   4518 O  OG  . SER B 1 289 ? 33.005  4.685   43.399  1.00 18.89 ? 289 SER B OG  1 
ATOM   4519 N  N   . LEU B 1 290 ? 31.997  1.671   41.698  1.00 19.39 ? 290 LEU B N   1 
ATOM   4520 C  CA  . LEU B 1 290 ? 31.066  0.677   42.194  1.00 19.75 ? 290 LEU B CA  1 
ATOM   4521 C  C   . LEU B 1 290 ? 30.601  1.059   43.585  1.00 19.80 ? 290 LEU B C   1 
ATOM   4522 O  O   . LEU B 1 290 ? 29.409  1.002   43.861  1.00 17.76 ? 290 LEU B O   1 
ATOM   4523 C  CB  . LEU B 1 290 ? 31.741  -0.683  42.212  1.00 18.48 ? 290 LEU B CB  1 
ATOM   4524 C  CG  . LEU B 1 290 ? 30.887  -1.790  42.815  1.00 22.96 ? 290 LEU B CG  1 
ATOM   4525 C  CD1 . LEU B 1 290 ? 29.736  -2.098  41.912  1.00 25.69 ? 290 LEU B CD1 1 
ATOM   4526 C  CD2 . LEU B 1 290 ? 31.699  -3.062  43.033  1.00 28.44 ? 290 LEU B CD2 1 
ATOM   4527 N  N   . GLN B 1 291 ? 31.506  1.556   44.438  1.00 20.56 ? 291 GLN B N   1 
ATOM   4528 C  CA  . GLN B 1 291 ? 31.100  1.983   45.776  1.00 19.96 ? 291 GLN B CA  1 
ATOM   4529 C  C   . GLN B 1 291 ? 30.130  3.165   45.695  1.00 17.95 ? 291 GLN B C   1 
ATOM   4530 O  O   . GLN B 1 291 ? 29.175  3.189   46.459  1.00 17.40 ? 291 GLN B O   1 
ATOM   4531 C  CB  . GLN B 1 291 ? 32.280  2.360   46.682  1.00 23.83 ? 291 GLN B CB  1 
ATOM   4532 C  CG  . GLN B 1 291 ? 31.832  2.514   48.152  1.00 29.89 ? 291 GLN B CG  1 
ATOM   4533 C  CD  . GLN B 1 291 ? 31.199  1.258   48.761  1.00 45.47 ? 291 GLN B CD  1 
ATOM   4534 O  OE1 . GLN B 1 291 ? 31.858  0.215   48.901  1.00 40.16 ? 291 GLN B OE1 1 
ATOM   4535 N  NE2 . GLN B 1 291 ? 29.894  1.306   49.092  1.00 43.10 ? 291 GLN B NE2 1 
ATOM   4536 N  N   . GLU B 1 292 ? 30.384  4.141   44.816  1.00 18.67 ? 292 GLU B N   1 
ATOM   4537 C  CA  . GLU B 1 292 ? 29.498  5.288   44.665  1.00 19.97 ? 292 GLU B CA  1 
ATOM   4538 C  C   . GLU B 1 292 ? 28.107  4.819   44.226  1.00 16.03 ? 292 GLU B C   1 
ATOM   4539 O  O   . GLU B 1 292 ? 27.131  5.296   44.739  1.00 16.27 ? 292 GLU B O   1 
ATOM   4540 C  CB  . GLU B 1 292 ? 30.007  6.323   43.665  1.00 22.01 ? 292 GLU B CB  1 
ATOM   4541 C  CG  . GLU B 1 292 ? 31.017  7.292   44.245  1.00 33.44 ? 292 GLU B CG  1 
ATOM   4542 C  CD  . GLU B 1 292 ? 31.860  8.072   43.239  1.00 39.22 ? 292 GLU B CD  1 
ATOM   4543 O  OE1 . GLU B 1 292 ? 32.148  7.566   42.118  1.00 34.41 ? 292 GLU B OE1 1 
ATOM   4544 O  OE2 . GLU B 1 292 ? 32.352  9.138   43.627  1.00 52.51 ? 292 GLU B OE2 1 
ATOM   4545 N  N   . GLN B 1 293 ? 28.052  3.877   43.285  1.00 15.80 ? 293 GLN B N   1 
ATOM   4546 C  CA  . GLN B 1 293 ? 26.768  3.395   42.757  1.00 15.81 ? 293 GLN B CA  1 
ATOM   4547 C  C   . GLN B 1 293 ? 25.967  2.695   43.836  1.00 17.36 ? 293 GLN B C   1 
ATOM   4548 O  O   . GLN B 1 293 ? 24.754  2.902   43.997  1.00 16.24 ? 293 GLN B O   1 
ATOM   4549 C  CB  . GLN B 1 293 ? 27.005  2.451   41.560  1.00 14.68 ? 293 GLN B CB  1 
ATOM   4550 C  CG  . GLN B 1 293 ? 27.642  3.137   40.347  1.00 14.71 ? 293 GLN B CG  1 
ATOM   4551 C  CD  . GLN B 1 293 ? 27.654  2.223   39.129  1.00 15.90 ? 293 GLN B CD  1 
ATOM   4552 O  OE1 . GLN B 1 293 ? 27.115  1.112   39.212  1.00 16.28 ? 293 GLN B OE1 1 
ATOM   4553 N  NE2 . GLN B 1 293 ? 28.209  2.680   37.999  1.00 19.31 ? 293 GLN B NE2 1 
ATOM   4554 N  N   . GLU B 1 294 ? 26.661  1.827   44.612  1.00 17.03 ? 294 GLU B N   1 
ATOM   4555 C  CA  . GLU B 1 294 ? 25.989  1.117   45.667  1.00 16.18 ? 294 GLU B CA  1 
ATOM   4556 C  C   . GLU B 1 294 ? 25.549  2.094   46.747  1.00 17.61 ? 294 GLU B C   1 
ATOM   4557 O  O   . GLU B 1 294 ? 24.461  1.908   47.291  1.00 20.62 ? 294 GLU B O   1 
ATOM   4558 C  CB  . GLU B 1 294 ? 26.880  -0.029  46.201  1.00 16.36 ? 294 GLU B CB  1 
ATOM   4559 C  CG  . GLU B 1 294 ? 27.138  -1.082  45.172  1.00 17.42 ? 294 GLU B CG  1 
ATOM   4560 C  CD  . GLU B 1 294 ? 27.977  -2.251  45.597  1.00 19.36 ? 294 GLU B CD  1 
ATOM   4561 O  OE1 . GLU B 1 294 ? 28.607  -2.080  46.626  1.00 20.20 ? 294 GLU B OE1 1 
ATOM   4562 O  OE2 . GLU B 1 294 ? 27.882  -3.344  44.954  1.00 16.95 ? 294 GLU B OE2 1 
ATOM   4563 N  N   . ASP B 1 295 ? 26.396  3.071   47.086  1.00 17.86 ? 295 ASP B N   1 
ATOM   4564 C  CA  . ASP B 1 295 ? 26.033  4.019   48.110  1.00 15.64 ? 295 ASP B CA  1 
ATOM   4565 C  C   . ASP B 1 295 ? 24.826  4.857   47.702  1.00 16.72 ? 295 ASP B C   1 
ATOM   4566 O  O   . ASP B 1 295 ? 24.060  5.211   48.572  1.00 19.88 ? 295 ASP B O   1 
ATOM   4567 C  CB  . ASP B 1 295 ? 27.158  4.987   48.407  1.00 20.14 ? 295 ASP B CB  1 
ATOM   4568 C  CG  . ASP B 1 295 ? 28.265  4.448   49.309  1.00 26.84 ? 295 ASP B CG  1 
ATOM   4569 O  OD1 . ASP B 1 295 ? 28.107  3.364   49.906  1.00 24.24 ? 295 ASP B OD1 1 
ATOM   4570 O  OD2 . ASP B 1 295 ? 29.263  5.128   49.379  1.00 29.45 ? 295 ASP B OD2 1 
ATOM   4571 N  N   . VAL B 1 296 ? 24.663  5.169   46.397  1.00 16.55 ? 296 VAL B N   1 
ATOM   4572 C  CA  . VAL B 1 296 ? 23.460  5.873   45.924  1.00 15.64 ? 296 VAL B CA  1 
ATOM   4573 C  C   . VAL B 1 296 ? 22.170  5.148   46.290  1.00 14.53 ? 296 VAL B C   1 
ATOM   4574 O  O   . VAL B 1 296 ? 21.167  5.812   46.605  1.00 16.36 ? 296 VAL B O   1 
ATOM   4575 C  CB  . VAL B 1 296 ? 23.558  6.076   44.400  1.00 16.80 ? 296 VAL B CB  1 
ATOM   4576 C  CG1 . VAL B 1 296 ? 22.180  6.329   43.807  1.00 19.77 ? 296 VAL B CG1 1 
ATOM   4577 C  CG2 . VAL B 1 296 ? 24.573  7.156   44.060  1.00 17.10 ? 296 VAL B CG2 1 
ATOM   4578 N  N   . PHE B 1 297 ? 22.156  3.798   46.201  1.00 14.04 ? 297 PHE B N   1 
ATOM   4579 C  CA  . PHE B 1 297 ? 20.943  3.019   46.379  1.00 15.52 ? 297 PHE B CA  1 
ATOM   4580 C  C   . PHE B 1 297 ? 20.783  2.497   47.791  1.00 16.94 ? 297 PHE B C   1 
ATOM   4581 O  O   . PHE B 1 297 ? 19.652  2.462   48.318  1.00 17.20 ? 297 PHE B O   1 
ATOM   4582 C  CB  . PHE B 1 297 ? 20.810  1.870   45.372  1.00 16.12 ? 297 PHE B CB  1 
ATOM   4583 C  CG  . PHE B 1 297 ? 20.430  2.396   44.012  1.00 15.76 ? 297 PHE B CG  1 
ATOM   4584 C  CD1 . PHE B 1 297 ? 19.148  2.964   43.850  1.00 16.89 ? 297 PHE B CD1 1 
ATOM   4585 C  CD2 . PHE B 1 297 ? 21.301  2.374   42.967  1.00 16.96 ? 297 PHE B CD2 1 
ATOM   4586 C  CE1 . PHE B 1 297 ? 18.787  3.507   42.649  1.00 15.54 ? 297 PHE B CE1 1 
ATOM   4587 C  CE2 . PHE B 1 297 ? 20.919  2.856   41.709  1.00 16.85 ? 297 PHE B CE2 1 
ATOM   4588 C  CZ  . PHE B 1 297 ? 19.690  3.461   41.594  1.00 18.29 ? 297 PHE B CZ  1 
ATOM   4589 N  N   . GLY B 1 298 ? 21.895  2.122   48.427  1.00 16.46 ? 298 GLY B N   1 
ATOM   4590 C  CA  . GLY B 1 298 ? 21.754  1.433   49.692  1.00 17.69 ? 298 GLY B CA  1 
ATOM   4591 C  C   . GLY B 1 298 ? 21.685  -0.090  49.576  1.00 19.21 ? 298 GLY B C   1 
ATOM   4592 O  O   . GLY B 1 298 ? 21.437  -0.797  50.566  1.00 17.80 ? 298 GLY B O   1 
ATOM   4593 N  N   . ARG B 1 299 ? 21.892  -0.604  48.362  1.00 17.94 ? 299 ARG B N   1 
ATOM   4594 C  CA  . ARG B 1 299 ? 21.919  -2.022  48.094  1.00 16.10 ? 299 ARG B CA  1 
ATOM   4595 C  C   . ARG B 1 299 ? 23.153  -2.291  47.236  1.00 19.78 ? 299 ARG B C   1 
ATOM   4596 O  O   . ARG B 1 299 ? 23.617  -1.400  46.541  1.00 17.02 ? 299 ARG B O   1 
ATOM   4597 C  CB  . ARG B 1 299 ? 20.648  -2.456  47.334  1.00 15.69 ? 299 ARG B CB  1 
ATOM   4598 C  CG  . ARG B 1 299 ? 19.361  -2.463  48.113  1.00 16.80 ? 299 ARG B CG  1 
ATOM   4599 C  CD  . ARG B 1 299 ? 18.225  -2.815  47.236  1.00 16.43 ? 299 ARG B CD  1 
ATOM   4600 N  NE  . ARG B 1 299 ? 16.958  -2.965  47.932  1.00 17.18 ? 299 ARG B NE  1 
ATOM   4601 C  CZ  . ARG B 1 299 ? 16.523  -4.048  48.551  1.00 18.04 ? 299 ARG B CZ  1 
ATOM   4602 N  NH1 . ARG B 1 299 ? 17.248  -5.184  48.562  1.00 16.38 ? 299 ARG B NH1 1 
ATOM   4603 N  NH2 . ARG B 1 299 ? 15.361  -3.972  49.192  1.00 18.17 ? 299 ARG B NH2 1 
ATOM   4604 N  N   . ASP B 1 300 ? 23.657  -3.539  47.266  1.00 17.16 ? 300 ASP B N   1 
ATOM   4605 C  CA  . ASP B 1 300 ? 24.815  -3.861  46.456  1.00 19.91 ? 300 ASP B CA  1 
ATOM   4606 C  C   . ASP B 1 300 ? 24.304  -4.179  45.056  1.00 18.38 ? 300 ASP B C   1 
ATOM   4607 O  O   . ASP B 1 300 ? 23.134  -4.505  44.853  1.00 18.90 ? 300 ASP B O   1 
ATOM   4608 C  CB  . ASP B 1 300 ? 25.647  -5.007  47.068  1.00 22.03 ? 300 ASP B CB  1 
ATOM   4609 C  CG  . ASP B 1 300 ? 24.979  -6.366  46.905  1.00 24.76 ? 300 ASP B CG  1 
ATOM   4610 O  OD1 . ASP B 1 300 ? 24.086  -6.647  47.623  1.00 28.65 ? 300 ASP B OD1 1 
ATOM   4611 O  OD2 . ASP B 1 300 ? 25.362  -7.114  45.990  1.00 31.98 ? 300 ASP B OD2 1 
ATOM   4612 N  N   . LYS B 1 301 ? 25.208  -4.088  44.084  1.00 18.12 ? 301 LYS B N   1 
ATOM   4613 C  CA  . LYS B 1 301 ? 24.805  -4.168  42.683  1.00 18.04 ? 301 LYS B CA  1 
ATOM   4614 C  C   . LYS B 1 301 ? 24.632  -5.638  42.280  1.00 21.44 ? 301 LYS B C   1 
ATOM   4615 O  O   . LYS B 1 301 ? 23.759  -5.947  41.535  1.00 23.06 ? 301 LYS B O   1 
ATOM   4616 C  CB  . LYS B 1 301 ? 25.842  -3.435  41.839  1.00 19.36 ? 301 LYS B CB  1 
ATOM   4617 C  CG  . LYS B 1 301 ? 25.402  -3.233  40.400  1.00 19.16 ? 301 LYS B CG  1 
ATOM   4618 C  CD  . LYS B 1 301 ? 26.250  -2.249  39.603  1.00 18.28 ? 301 LYS B CD  1 
ATOM   4619 C  CE  . LYS B 1 301 ? 25.524  -1.860  38.349  1.00 15.59 ? 301 LYS B CE  1 
ATOM   4620 N  NZ  . LYS B 1 301 ? 26.329  -0.964  37.516  1.00 16.13 ? 301 LYS B NZ  1 
ATOM   4621 N  N   . GLY B 1 302 ? 25.499  -6.548  42.745  1.00 21.36 ? 302 GLY B N   1 
ATOM   4622 C  CA  . GLY B 1 302 ? 25.478  -7.948  42.298  1.00 23.42 ? 302 GLY B CA  1 
ATOM   4623 C  C   . GLY B 1 302 ? 24.252  -8.720  42.766  1.00 22.93 ? 302 GLY B C   1 
ATOM   4624 O  O   . GLY B 1 302 ? 23.505  -9.295  41.971  1.00 22.21 ? 302 GLY B O   1 
ATOM   4625 N  N   . GLU B 1 303 ? 24.004  -8.672  44.050  1.00 20.89 ? 303 GLU B N   1 
ATOM   4626 C  CA  . GLU B 1 303 ? 22.922  -9.448  44.645  1.00 21.38 ? 303 GLU B CA  1 
ATOM   4627 C  C   . GLU B 1 303 ? 21.700  -8.526  44.804  1.00 21.99 ? 303 GLU B C   1 
ATOM   4628 O  O   . GLU B 1 303 ? 20.548  -8.970  44.806  1.00 21.42 ? 303 GLU B O   1 
ATOM   4629 C  CB  . GLU B 1 303 ? 23.290  -10.043 46.026  1.00 23.55 ? 303 GLU B CB  1 
ATOM   4630 C  CG  . GLU B 1 303 ? 22.144  -10.684 46.814  1.00 24.30 ? 303 GLU B CG  1 
ATOM   4631 C  CD  . GLU B 1 303 ? 21.441  -11.885 46.171  1.00 31.29 ? 303 GLU B CD  1 
ATOM   4632 O  OE1 . GLU B 1 303 ? 22.012  -12.478 45.264  1.00 32.41 ? 303 GLU B OE1 1 
ATOM   4633 O  OE2 . GLU B 1 303 ? 20.294  -12.241 46.538  1.00 26.64 ? 303 GLU B OE2 1 
ATOM   4634 N  N   . GLY B 1 304 ? 21.937  -7.223  44.977  1.00 20.28 ? 304 GLY B N   1 
ATOM   4635 C  CA  . GLY B 1 304 ? 20.856  -6.343  45.345  1.00 15.53 ? 304 GLY B CA  1 
ATOM   4636 C  C   . GLY B 1 304 ? 20.357  -6.480  46.775  1.00 16.68 ? 304 GLY B C   1 
ATOM   4637 O  O   . GLY B 1 304 ? 19.220  -6.118  47.092  1.00 17.71 ? 304 GLY B O   1 
ATOM   4638 N  N   . ALA B 1 305 ? 21.210  -7.006  47.660  1.00 18.83 ? 305 ALA B N   1 
ATOM   4639 C  CA  . ALA B 1 305 ? 20.932  -7.033  49.073  1.00 19.65 ? 305 ALA B CA  1 
ATOM   4640 C  C   . ALA B 1 305 ? 21.076  -5.641  49.688  1.00 15.92 ? 305 ALA B C   1 
ATOM   4641 O  O   . ALA B 1 305 ? 21.965  -4.877  49.287  1.00 16.15 ? 305 ALA B O   1 
ATOM   4642 C  CB  . ALA B 1 305 ? 21.937  -7.972  49.744  1.00 19.57 ? 305 ALA B CB  1 
ATOM   4643 N  N   . PRO B 1 306 ? 20.268  -5.302  50.712  1.00 17.17 ? 306 PRO B N   1 
ATOM   4644 C  CA  . PRO B 1 306 ? 20.486  -4.090  51.485  1.00 19.90 ? 306 PRO B CA  1 
ATOM   4645 C  C   . PRO B 1 306 ? 21.871  -4.145  52.109  1.00 20.96 ? 306 PRO B C   1 
ATOM   4646 O  O   . PRO B 1 306 ? 22.399  -5.228  52.370  1.00 26.20 ? 306 PRO B O   1 
ATOM   4647 C  CB  . PRO B 1 306 ? 19.447  -4.128  52.615  1.00 19.25 ? 306 PRO B CB  1 
ATOM   4648 C  CG  . PRO B 1 306 ? 18.389  -5.091  52.118  1.00 19.84 ? 306 PRO B CG  1 
ATOM   4649 C  CD  . PRO B 1 306 ? 19.141  -6.080  51.235  1.00 16.55 ? 306 PRO B CD  1 
ATOM   4650 N  N   . VAL B 1 307 ? 22.492  -2.997  52.239  1.00 21.30 ? 307 VAL B N   1 
ATOM   4651 C  CA  . VAL B 1 307 ? 23.796  -2.915  52.901  1.00 25.00 ? 307 VAL B CA  1 
ATOM   4652 C  C   . VAL B 1 307 ? 23.719  -3.676  54.250  1.00 31.49 ? 307 VAL B C   1 
ATOM   4653 O  O   . VAL B 1 307 ? 22.804  -3.515  55.082  1.00 23.92 ? 307 VAL B O   1 
ATOM   4654 C  CB  . VAL B 1 307 ? 24.261  -1.451  53.073  1.00 30.87 ? 307 VAL B CB  1 
ATOM   4655 C  CG1 . VAL B 1 307 ? 23.185  -0.633  53.713  1.00 32.22 ? 307 VAL B CG1 1 
ATOM   4656 C  CG2 . VAL B 1 307 ? 25.538  -1.289  53.918  1.00 36.22 ? 307 VAL B CG2 1 
ATOM   4657 N  N   . GLY B 1 308 ? 24.736  -4.523  54.449  1.00 30.00 ? 308 GLY B N   1 
ATOM   4658 C  CA  . GLY B 1 308 ? 24.953  -5.244  55.684  1.00 32.69 ? 308 GLY B CA  1 
ATOM   4659 C  C   . GLY B 1 308 ? 24.154  -6.542  55.709  1.00 33.64 ? 308 GLY B C   1 
ATOM   4660 O  O   . GLY B 1 308 ? 24.243  -7.239  56.705  1.00 34.26 ? 308 GLY B O   1 
ATOM   4661 N  N   . LYS B 1 309 ? 23.397  -6.858  54.628  1.00 28.23 ? 309 LYS B N   1 
ATOM   4662 C  CA  . LYS B 1 309 ? 22.599  -8.063  54.559  1.00 26.30 ? 309 LYS B CA  1 
ATOM   4663 C  C   . LYS B 1 309 ? 23.128  -8.921  53.431  1.00 31.03 ? 309 LYS B C   1 
ATOM   4664 O  O   . LYS B 1 309 ? 23.961  -8.498  52.638  1.00 37.84 ? 309 LYS B O   1 
ATOM   4665 C  CB  . LYS B 1 309 ? 21.110  -7.742  54.362  1.00 31.99 ? 309 LYS B CB  1 
ATOM   4666 C  CG  . LYS B 1 309 ? 20.447  -6.984  55.497  1.00 37.77 ? 309 LYS B CG  1 
ATOM   4667 C  CD  . LYS B 1 309 ? 20.596  -7.695  56.821  1.00 36.74 ? 309 LYS B CD  1 
ATOM   4668 C  CE  . LYS B 1 309 ? 20.058  -6.942  58.000  1.00 39.35 ? 309 LYS B CE  1 
ATOM   4669 N  NZ  . LYS B 1 309 ? 18.589  -6.884  57.942  1.00 41.63 ? 309 LYS B NZ  1 
ATOM   4670 N  N   . ALA B 1 310 ? 22.615  -10.143 53.351  1.00 32.45 ? 310 ALA B N   1 
ATOM   4671 C  CA  . ALA B 1 310 ? 23.197  -11.122 52.476  1.00 32.40 ? 310 ALA B CA  1 
ATOM   4672 C  C   . ALA B 1 310 ? 22.354  -11.354 51.220  1.00 30.11 ? 310 ALA B C   1 
ATOM   4673 O  O   . ALA B 1 310 ? 22.939  -11.718 50.208  1.00 33.45 ? 310 ALA B O   1 
ATOM   4674 C  CB  . ALA B 1 310 ? 23.385  -12.389 53.269  1.00 30.19 ? 310 ALA B CB  1 
ATOM   4675 N  N   . LYS B 1 311 ? 21.006  -11.243 51.272  1.00 31.47 ? 311 LYS B N   1 
ATOM   4676 C  CA  . LYS B 1 311 ? 20.177  -11.656 50.137  1.00 28.88 ? 311 LYS B CA  1 
ATOM   4677 C  C   . LYS B 1 311 ? 19.289  -10.492 49.679  1.00 24.70 ? 311 LYS B C   1 
ATOM   4678 O  O   . LYS B 1 311 ? 18.927  -9.631  50.492  1.00 24.19 ? 311 LYS B O   1 
ATOM   4679 C  CB  . LYS B 1 311 ? 19.330  -12.884 50.497  1.00 27.50 ? 311 LYS B CB  1 
ATOM   4680 C  CG  . LYS B 1 311 ? 20.085  -14.027 51.164  1.00 28.32 ? 311 LYS B CG  1 
ATOM   4681 N  N   . GLU B 1 312 ? 18.957  -10.485 48.389  1.00 22.73 ? 312 GLU B N   1 
ATOM   4682 C  CA  . GLU B 1 312 ? 18.095  -9.476  47.784  1.00 21.51 ? 312 GLU B CA  1 
ATOM   4683 C  C   . GLU B 1 312 ? 16.875  -9.178  48.654  1.00 19.94 ? 312 GLU B C   1 
ATOM   4684 O  O   . GLU B 1 312 ? 16.591  -7.993  48.958  1.00 21.71 ? 312 GLU B O   1 
ATOM   4685 C  CB  . GLU B 1 312 ? 17.631  -9.942  46.402  1.00 21.93 ? 312 GLU B CB  1 
ATOM   4686 C  CG  . GLU B 1 312 ? 16.756  -8.916  45.678  1.00 21.35 ? 312 GLU B CG  1 
ATOM   4687 C  CD  . GLU B 1 312 ? 16.076  -9.389  44.400  1.00 21.19 ? 312 GLU B CD  1 
ATOM   4688 O  OE1 . GLU B 1 312 ? 16.453  -10.490 43.873  1.00 20.52 ? 312 GLU B OE1 1 
ATOM   4689 O  OE2 . GLU B 1 312 ? 15.124  -8.740  43.982  1.00 20.27 ? 312 GLU B OE2 1 
ATOM   4690 N  N   . ARG B 1 313 ? 16.212  -10.250 49.106  1.00 18.05 ? 313 ARG B N   1 
ATOM   4691 C  CA  . ARG B 1 313 ? 14.920  -10.142 49.777  1.00 24.22 ? 313 ARG B CA  1 
ATOM   4692 C  C   . ARG B 1 313 ? 15.028  -9.945  51.285  1.00 20.61 ? 313 ARG B C   1 
ATOM   4693 O  O   . ARG B 1 313 ? 14.019  -9.672  51.931  1.00 24.49 ? 313 ARG B O   1 
ATOM   4694 C  CB  . ARG B 1 313 ? 13.958  -11.279 49.369  1.00 24.78 ? 313 ARG B CB  1 
ATOM   4695 C  CG  . ARG B 1 313 ? 13.446  -11.003 47.948  1.00 29.47 ? 313 ARG B CG  1 
ATOM   4696 C  CD  . ARG B 1 313 ? 12.095  -11.611 47.589  1.00 37.92 ? 313 ARG B CD  1 
ATOM   4697 N  NE  . ARG B 1 313 ? 11.777  -11.422 46.183  1.00 42.52 ? 313 ARG B NE  1 
ATOM   4698 C  CZ  . ARG B 1 313 ? 11.234  -10.320 45.666  1.00 47.18 ? 313 ARG B CZ  1 
ATOM   4699 N  NH1 . ARG B 1 313 ? 10.622  -9.458  46.456  1.00 37.66 ? 313 ARG B NH1 1 
ATOM   4700 N  NH2 . ARG B 1 313 ? 11.288  -10.100 44.358  1.00 47.79 ? 313 ARG B NH2 1 
ATOM   4701 N  N   . ASP B 1 314 ? 16.239  -9.920  51.823  1.00 23.35 ? 314 ASP B N   1 
ATOM   4702 C  CA  . ASP B 1 314 ? 16.362  -9.535  53.219  1.00 24.50 ? 314 ASP B CA  1 
ATOM   4703 C  C   . ASP B 1 314 ? 15.868  -8.103  53.404  1.00 25.88 ? 314 ASP B C   1 
ATOM   4704 O  O   . ASP B 1 314 ? 16.143  -7.214  52.572  1.00 22.34 ? 314 ASP B O   1 
ATOM   4705 C  CB  . ASP B 1 314 ? 17.807  -9.634  53.702  1.00 26.72 ? 314 ASP B CB  1 
ATOM   4706 C  CG  . ASP B 1 314 ? 18.377  -11.037 53.808  1.00 25.48 ? 314 ASP B CG  1 
ATOM   4707 O  OD1 . ASP B 1 314 ? 17.578  -12.015 53.811  1.00 31.84 ? 314 ASP B OD1 1 
ATOM   4708 O  OD2 . ASP B 1 314 ? 19.592  -11.147 53.741  1.00 26.54 ? 314 ASP B OD2 1 
ATOM   4709 N  N   . GLU B 1 315 ? 15.154  -7.894  54.511  1.00 26.27 ? 315 GLU B N   1 
ATOM   4710 C  CA  . GLU B 1 315 ? 14.526  -6.599  54.786  1.00 27.15 ? 315 GLU B CA  1 
ATOM   4711 C  C   . GLU B 1 315 ? 15.638  -5.592  55.114  1.00 25.21 ? 315 GLU B C   1 
ATOM   4712 O  O   . GLU B 1 315 ? 16.699  -5.909  55.716  1.00 23.80 ? 315 GLU B O   1 
ATOM   4713 C  CB  . GLU B 1 315 ? 13.421  -6.714  55.850  1.00 35.18 ? 315 GLU B CB  1 
ATOM   4714 C  CG  . GLU B 1 315 ? 12.107  -7.348  55.336  1.00 35.77 ? 315 GLU B CG  1 
ATOM   4715 C  CD  . GLU B 1 315 ? 11.469  -6.693  54.095  1.00 40.52 ? 315 GLU B CD  1 
ATOM   4716 O  OE1 . GLU B 1 315 ? 11.311  -5.474  54.100  1.00 42.33 ? 315 GLU B OE1 1 
ATOM   4717 O  OE2 . GLU B 1 315 ? 11.101  -7.391  53.135  1.00 43.09 ? 315 GLU B OE2 1 
ATOM   4718 N  N   . PRO B 1 316 ? 15.508  -4.363  54.588  1.00 24.83 ? 316 PRO B N   1 
ATOM   4719 C  CA  . PRO B 1 316 ? 16.569  -3.376  54.741  1.00 24.76 ? 316 PRO B CA  1 
ATOM   4720 C  C   . PRO B 1 316 ? 16.687  -2.938  56.183  1.00 25.15 ? 316 PRO B C   1 
ATOM   4721 O  O   . PRO B 1 316 ? 15.710  -2.934  56.919  1.00 24.80 ? 316 PRO B O   1 
ATOM   4722 C  CB  . PRO B 1 316 ? 16.101  -2.154  53.921  1.00 25.15 ? 316 PRO B CB  1 
ATOM   4723 C  CG  . PRO B 1 316 ? 14.780  -2.482  53.346  1.00 23.81 ? 316 PRO B CG  1 
ATOM   4724 C  CD  . PRO B 1 316 ? 14.388  -3.887  53.742  1.00 25.54 ? 316 PRO B CD  1 
ATOM   4725 N  N   . PHE B 1 317 ? 17.893  -2.532  56.560  1.00 27.98 ? 317 PHE B N   1 
ATOM   4726 C  CA  . PHE B 1 317 ? 18.128  -1.844  57.814  1.00 23.68 ? 317 PHE B CA  1 
ATOM   4727 C  C   . PHE B 1 317 ? 18.522  -0.419  57.436  1.00 19.66 ? 317 PHE B C   1 
ATOM   4728 O  O   . PHE B 1 317 ? 19.623  -0.174  56.957  1.00 20.85 ? 317 PHE B O   1 
ATOM   4729 C  CB  . PHE B 1 317 ? 19.142  -2.646  58.653  1.00 27.19 ? 317 PHE B CB  1 
ATOM   4730 C  CG  . PHE B 1 317 ? 19.469  -1.975  59.954  1.00 35.03 ? 317 PHE B CG  1 
ATOM   4731 C  CD1 . PHE B 1 317 ? 18.465  -1.600  60.833  1.00 41.17 ? 317 PHE B CD1 1 
ATOM   4732 C  CD2 . PHE B 1 317 ? 20.781  -1.645  60.264  1.00 37.30 ? 317 PHE B CD2 1 
ATOM   4733 C  CE1 . PHE B 1 317 ? 18.792  -0.952  62.019  1.00 45.05 ? 317 PHE B CE1 1 
ATOM   4734 C  CE2 . PHE B 1 317 ? 21.103  -1.007  61.457  1.00 37.88 ? 317 PHE B CE2 1 
ATOM   4735 C  CZ  . PHE B 1 317 ? 20.102  -0.628  62.314  1.00 41.36 ? 317 PHE B CZ  1 
ATOM   4736 N  N   . LEU B 1 318 ? 17.589  0.519   57.528  1.00 19.24 ? 318 LEU B N   1 
ATOM   4737 C  CA  . LEU B 1 318 ? 17.743  1.812   56.885  1.00 19.97 ? 318 LEU B CA  1 
ATOM   4738 C  C   . LEU B 1 318 ? 18.878  2.582   57.536  1.00 24.98 ? 318 LEU B C   1 
ATOM   4739 O  O   . LEU B 1 318 ? 19.537  3.337   56.839  1.00 21.14 ? 318 LEU B O   1 
ATOM   4740 C  CB  . LEU B 1 318 ? 16.439  2.603   56.964  1.00 22.89 ? 318 LEU B CB  1 
ATOM   4741 C  CG  . LEU B 1 318 ? 15.245  1.926   56.276  1.00 22.69 ? 318 LEU B CG  1 
ATOM   4742 C  CD1 . LEU B 1 318 ? 14.008  2.808   56.383  1.00 30.51 ? 318 LEU B CD1 1 
ATOM   4743 C  CD2 . LEU B 1 318 ? 15.601  1.641   54.820  1.00 25.54 ? 318 LEU B CD2 1 
ATOM   4744 N  N   . LYS B 1 319 ? 19.139  2.398   58.853  1.00 25.34 ? 319 LYS B N   1 
ATOM   4745 C  CA  . LYS B 1 319 ? 20.217  3.186   59.462  1.00 30.58 ? 319 LYS B CA  1 
ATOM   4746 C  C   . LYS B 1 319 ? 21.612  2.816   58.953  1.00 25.00 ? 319 LYS B C   1 
ATOM   4747 O  O   . LYS B 1 319 ? 22.545  3.565   59.160  1.00 25.52 ? 319 LYS B O   1 
ATOM   4748 C  CB  . LYS B 1 319 ? 20.244  3.028   60.987  1.00 35.91 ? 319 LYS B CB  1 
ATOM   4749 C  CG  . LYS B 1 319 ? 18.952  3.399   61.681  1.00 48.87 ? 319 LYS B CG  1 
ATOM   4750 C  CD  . LYS B 1 319 ? 18.632  4.880   61.655  1.00 47.80 ? 319 LYS B CD  1 
ATOM   4751 C  CE  . LYS B 1 319 ? 17.515  5.199   62.628  1.00 54.36 ? 319 LYS B CE  1 
ATOM   4752 N  NZ  . LYS B 1 319 ? 17.855  4.787   64.010  1.00 57.28 ? 319 LYS B NZ  1 
ATOM   4753 N  N   . ALA B 1 320 ? 21.798  1.702   58.266  1.00 23.94 ? 320 ALA B N   1 
ATOM   4754 C  CA  . ALA B 1 320 ? 23.085  1.308   57.742  1.00 21.67 ? 320 ALA B CA  1 
ATOM   4755 C  C   . ALA B 1 320 ? 23.353  1.992   56.409  1.00 20.61 ? 320 ALA B C   1 
ATOM   4756 O  O   . ALA B 1 320 ? 24.475  2.048   55.936  1.00 23.93 ? 320 ALA B O   1 
ATOM   4757 C  CB  . ALA B 1 320 ? 23.185  -0.181  57.589  1.00 22.28 ? 320 ALA B CB  1 
ATOM   4758 N  N   . MET B 1 321 ? 22.288  2.494   55.783  1.00 19.39 ? 321 MET B N   1 
ATOM   4759 C  CA  . MET B 1 321 ? 22.446  3.232   54.527  1.00 18.54 ? 321 MET B CA  1 
ATOM   4760 C  C   . MET B 1 321 ? 22.792  4.690   54.770  1.00 18.29 ? 321 MET B C   1 
ATOM   4761 O  O   . MET B 1 321 ? 22.463  5.285   55.783  1.00 19.02 ? 321 MET B O   1 
ATOM   4762 C  CB  . MET B 1 321 ? 21.179  3.150   53.680  1.00 16.27 ? 321 MET B CB  1 
ATOM   4763 C  CG  . MET B 1 321 ? 20.696  1.758   53.486  1.00 18.30 ? 321 MET B CG  1 
ATOM   4764 S  SD  . MET B 1 321 ? 19.062  1.849   52.665  1.00 19.96 ? 321 MET B SD  1 
ATOM   4765 C  CE  . MET B 1 321 ? 18.713  0.104   52.610  1.00 19.60 ? 321 MET B CE  1 
ATOM   4766 N  N   . LYS B 1 322 ? 23.394  5.291   53.738  1.00 19.60 ? 322 LYS B N   1 
ATOM   4767 C  CA  . LYS B 1 322 ? 23.680  6.717   53.773  1.00 22.26 ? 322 LYS B CA  1 
ATOM   4768 C  C   . LYS B 1 322 ? 22.352  7.435   53.938  1.00 19.49 ? 322 LYS B C   1 
ATOM   4769 O  O   . LYS B 1 322 ? 21.298  6.979   53.425  1.00 19.55 ? 322 LYS B O   1 
ATOM   4770 C  CB  . LYS B 1 322 ? 24.443  7.059   52.485  1.00 23.40 ? 322 LYS B CB  1 
ATOM   4771 C  CG  . LYS B 1 322 ? 25.847  6.469   52.409  1.00 31.91 ? 322 LYS B CG  1 
ATOM   4772 C  CD  . LYS B 1 322 ? 26.968  7.508   52.320  1.00 35.79 ? 322 LYS B CD  1 
ATOM   4773 C  CE  . LYS B 1 322 ? 28.381  6.947   52.267  1.00 38.67 ? 322 LYS B CE  1 
ATOM   4774 N  N   . PRO B 1 323 ? 22.320  8.620   54.585  1.00 19.34 ? 323 PRO B N   1 
ATOM   4775 C  CA  . PRO B 1 323 ? 21.032  9.308   54.829  1.00 17.38 ? 323 PRO B CA  1 
ATOM   4776 C  C   . PRO B 1 323 ? 20.263  9.699   53.572  1.00 16.33 ? 323 PRO B C   1 
ATOM   4777 O  O   . PRO B 1 323 ? 19.038  9.784   53.596  1.00 21.65 ? 323 PRO B O   1 
ATOM   4778 C  CB  . PRO B 1 323 ? 21.460  10.595  55.589  1.00 21.03 ? 323 PRO B CB  1 
ATOM   4779 C  CG  . PRO B 1 323 ? 22.672  10.146  56.289  1.00 21.40 ? 323 PRO B CG  1 
ATOM   4780 C  CD  . PRO B 1 323 ? 23.430  9.236   55.337  1.00 21.17 ? 323 PRO B CD  1 
ATOM   4781 N  N   . ASP B 1 324 ? 20.980  9.936   52.484  1.00 16.98 ? 324 ASP B N   1 
ATOM   4782 C  CA  . ASP B 1 324 ? 20.357  10.332  51.232  1.00 17.78 ? 324 ASP B CA  1 
ATOM   4783 C  C   . ASP B 1 324 ? 20.384  9.224   50.179  1.00 15.55 ? 324 ASP B C   1 
ATOM   4784 O  O   . ASP B 1 324 ? 20.213  9.486   48.974  1.00 18.61 ? 324 ASP B O   1 
ATOM   4785 C  CB  . ASP B 1 324 ? 21.037  11.584  50.707  1.00 19.17 ? 324 ASP B CB  1 
ATOM   4786 C  CG  . ASP B 1 324 ? 20.703  12.836  51.541  1.00 27.70 ? 324 ASP B CG  1 
ATOM   4787 O  OD1 . ASP B 1 324 ? 19.518  13.015  52.018  1.00 23.72 ? 324 ASP B OD1 1 
ATOM   4788 O  OD2 . ASP B 1 324 ? 21.634  13.637  51.718  1.00 29.04 ? 324 ASP B OD2 1 
ATOM   4789 N  N   . ALA B 1 325 ? 20.564  7.988   50.636  1.00 14.58 ? 325 ALA B N   1 
ATOM   4790 C  CA  . ALA B 1 325 ? 20.451  6.842   49.757  1.00 15.39 ? 325 ALA B CA  1 
ATOM   4791 C  C   . ALA B 1 325 ? 18.973  6.740   49.305  1.00 14.32 ? 325 ALA B C   1 
ATOM   4792 O  O   . ALA B 1 325 ? 18.019  6.938   50.067  1.00 14.09 ? 325 ALA B O   1 
ATOM   4793 C  CB  . ALA B 1 325 ? 20.927  5.584   50.419  1.00 17.52 ? 325 ALA B CB  1 
ATOM   4794 N  N   . HIS B 1 326 ? 18.816  6.336   48.052  1.00 12.45 ? 326 HIS B N   1 
ATOM   4795 C  CA  . HIS B 1 326 ? 17.496  6.294   47.433  1.00 13.64 ? 326 HIS B CA  1 
ATOM   4796 C  C   . HIS B 1 326 ? 16.524  5.381   48.202  1.00 13.16 ? 326 HIS B C   1 
ATOM   4797 O  O   . HIS B 1 326 ? 15.365  5.755   48.406  1.00 14.84 ? 326 HIS B O   1 
ATOM   4798 C  CB  . HIS B 1 326 ? 17.679  5.795   46.026  1.00 12.68 ? 326 HIS B CB  1 
ATOM   4799 C  CG  . HIS B 1 326 ? 16.398  5.694   45.250  1.00 11.52 ? 326 HIS B CG  1 
ATOM   4800 N  ND1 . HIS B 1 326 ? 15.736  6.806   44.796  1.00 13.73 ? 326 HIS B ND1 1 
ATOM   4801 C  CD2 . HIS B 1 326 ? 15.654  4.583   44.904  1.00 12.98 ? 326 HIS B CD2 1 
ATOM   4802 C  CE1 . HIS B 1 326 ? 14.621  6.437   44.165  1.00 13.21 ? 326 HIS B CE1 1 
ATOM   4803 N  NE2 . HIS B 1 326 ? 14.567  5.088   44.220  1.00 11.52 ? 326 HIS B NE2 1 
ATOM   4804 N  N   . VAL B 1 327 ? 16.974  4.169   48.526  1.00 14.02 ? 327 VAL B N   1 
ATOM   4805 C  CA  . VAL B 1 327 ? 16.081  3.217   49.211  1.00 14.77 ? 327 VAL B CA  1 
ATOM   4806 C  C   . VAL B 1 327 ? 15.664  3.764   50.556  1.00 15.49 ? 327 VAL B C   1 
ATOM   4807 O  O   . VAL B 1 327 ? 14.494  3.701   50.903  1.00 16.11 ? 327 VAL B O   1 
ATOM   4808 C  CB  . VAL B 1 327 ? 16.680  1.823   49.373  1.00 15.96 ? 327 VAL B CB  1 
ATOM   4809 C  CG1 . VAL B 1 327 ? 15.825  0.964   50.284  1.00 16.25 ? 327 VAL B CG1 1 
ATOM   4810 C  CG2 . VAL B 1 327 ? 16.777  1.201   48.011  1.00 18.03 ? 327 VAL B CG2 1 
ATOM   4811 N  N   . ARG B 1 328 ? 16.610  4.363   51.283  1.00 14.52 ? 328 ARG B N   1 
ATOM   4812 C  CA  . ARG B 1 328 ? 16.264  4.954   52.557  1.00 16.56 ? 328 ARG B CA  1 
ATOM   4813 C  C   . ARG B 1 328 ? 15.221  6.077   52.436  1.00 16.69 ? 328 ARG B C   1 
ATOM   4814 O  O   . ARG B 1 328 ? 14.282  6.136   53.235  1.00 17.24 ? 328 ARG B O   1 
ATOM   4815 C  CB  . ARG B 1 328 ? 17.568  5.403   53.232  1.00 17.82 ? 328 ARG B CB  1 
ATOM   4816 C  CG  . ARG B 1 328 ? 17.293  6.009   54.599  1.00 20.02 ? 328 ARG B CG  1 
ATOM   4817 C  CD  . ARG B 1 328 ? 18.625  6.130   55.338  1.00 22.61 ? 328 ARG B CD  1 
ATOM   4818 N  NE  . ARG B 1 328 ? 18.414  6.734   56.652  1.00 22.39 ? 328 ARG B NE  1 
ATOM   4819 C  CZ  . ARG B 1 328 ? 19.394  6.962   57.519  1.00 26.72 ? 328 ARG B CZ  1 
ATOM   4820 N  NH1 . ARG B 1 328 ? 20.636  6.553   57.291  1.00 24.79 ? 328 ARG B NH1 1 
ATOM   4821 N  NH2 . ARG B 1 328 ? 19.114  7.665   58.594  1.00 31.50 ? 328 ARG B NH2 1 
ATOM   4822 N  N   . LEU B 1 329 ? 15.380  6.998   51.466  1.00 14.98 ? 329 LEU B N   1 
ATOM   4823 C  CA  . LEU B 1 329 ? 14.412  8.061   51.284  1.00 15.69 ? 329 LEU B CA  1 
ATOM   4824 C  C   . LEU B 1 329 ? 13.054  7.573   50.789  1.00 14.87 ? 329 LEU B C   1 
ATOM   4825 O  O   . LEU B 1 329 ? 12.078  8.235   51.037  1.00 18.19 ? 329 LEU B O   1 
ATOM   4826 C  CB  . LEU B 1 329 ? 14.997  9.122   50.377  1.00 15.68 ? 329 LEU B CB  1 
ATOM   4827 C  CG  . LEU B 1 329 ? 16.203  9.848   50.945  1.00 17.60 ? 329 LEU B CG  1 
ATOM   4828 C  CD1 . LEU B 1 329 ? 16.767  10.717  49.836  1.00 18.41 ? 329 LEU B CD1 1 
ATOM   4829 C  CD2 . LEU B 1 329 ? 15.814  10.688  52.172  1.00 20.88 ? 329 LEU B CD2 1 
ATOM   4830 N  N   . ALA B 1 330 ? 13.011  6.519   49.963  1.00 13.61 ? 330 ALA B N   1 
ATOM   4831 C  CA  . ALA B 1 330 ? 11.775  6.138   49.305  1.00 14.90 ? 330 ALA B CA  1 
ATOM   4832 C  C   . ALA B 1 330 ? 10.969  5.127   50.125  1.00 17.55 ? 330 ALA B C   1 
ATOM   4833 O  O   . ALA B 1 330 ? 9.797   4.899   49.838  1.00 14.68 ? 330 ALA B O   1 
ATOM   4834 C  CB  . ALA B 1 330 ? 12.092  5.496   47.970  1.00 15.40 ? 330 ALA B CB  1 
ATOM   4835 N  N   . HIS B 1 331 ? 11.603  4.499   51.114  1.00 15.62 ? 331 HIS B N   1 
ATOM   4836 C  CA  . HIS B 1 331 ? 10.983  3.439   51.899  1.00 15.82 ? 331 HIS B CA  1 
ATOM   4837 C  C   . HIS B 1 331 ? 9.745   3.948   52.644  1.00 16.23 ? 331 HIS B C   1 
ATOM   4838 O  O   . HIS B 1 331 ? 9.754   5.073   53.124  1.00 15.43 ? 331 HIS B O   1 
ATOM   4839 C  CB  . HIS B 1 331 ? 11.997  2.933   52.921  1.00 16.45 ? 331 HIS B CB  1 
ATOM   4840 C  CG  . HIS B 1 331 ? 11.640  1.662   53.616  1.00 21.85 ? 331 HIS B CG  1 
ATOM   4841 N  ND1 . HIS B 1 331 ? 10.752  1.584   54.690  1.00 20.03 ? 331 HIS B ND1 1 
ATOM   4842 C  CD2 . HIS B 1 331 ? 12.121  0.406   53.388  1.00 19.39 ? 331 HIS B CD2 1 
ATOM   4843 C  CE1 . HIS B 1 331 ? 10.725  0.315   55.106  1.00 22.05 ? 331 HIS B CE1 1 
ATOM   4844 N  NE2 . HIS B 1 331 ? 11.505  -0.438  54.280  1.00 20.93 ? 331 HIS B NE2 1 
ATOM   4845 N  N   . PRO B 1 332 ? 8.670   3.152   52.763  1.00 16.55 ? 332 PRO B N   1 
ATOM   4846 C  CA  . PRO B 1 332 ? 7.464   3.581   53.461  1.00 18.22 ? 332 PRO B CA  1 
ATOM   4847 C  C   . PRO B 1 332 ? 7.730   4.150   54.859  1.00 18.97 ? 332 PRO B C   1 
ATOM   4848 O  O   . PRO B 1 332 ? 7.056   5.110   55.228  1.00 19.91 ? 332 PRO B O   1 
ATOM   4849 C  CB  . PRO B 1 332 ? 6.593   2.310   53.507  1.00 16.33 ? 332 PRO B CB  1 
ATOM   4850 C  CG  . PRO B 1 332 ? 7.042   1.544   52.264  1.00 17.28 ? 332 PRO B CG  1 
ATOM   4851 C  CD  . PRO B 1 332 ? 8.489   1.867   52.062  1.00 16.68 ? 332 PRO B CD  1 
ATOM   4852 N  N   . ASP B 1 333 ? 8.701   3.559   55.578  1.00 19.11 ? 333 ASP B N   1 
ATOM   4853 C  CA  . ASP B 1 333 ? 8.979   3.958   56.970  1.00 22.10 ? 333 ASP B CA  1 
ATOM   4854 C  C   . ASP B 1 333 ? 9.528   5.390   57.030  1.00 19.09 ? 333 ASP B C   1 
ATOM   4855 O  O   . ASP B 1 333 ? 9.474   6.041   58.081  1.00 24.18 ? 333 ASP B O   1 
ATOM   4856 C  CB  . ASP B 1 333 ? 9.933   2.996   57.688  1.00 24.47 ? 333 ASP B CB  1 
ATOM   4857 C  CG  . ASP B 1 333 ? 9.394   1.621   58.092  1.00 28.60 ? 333 ASP B CG  1 
ATOM   4858 O  OD1 . ASP B 1 333 ? 8.258   1.338   57.847  1.00 27.12 ? 333 ASP B OD1 1 
ATOM   4859 O  OD2 . ASP B 1 333 ? 10.196  0.803   58.648  1.00 31.55 ? 333 ASP B OD2 1 
ATOM   4860 N  N   . SER B 1 334 ? 10.115  5.910   55.930  1.00 19.06 ? 334 SER B N   1 
ATOM   4861 C  CA  . SER B 1 334 ? 10.626  7.280   55.847  1.00 18.37 ? 334 SER B CA  1 
ATOM   4862 C  C   . SER B 1 334 ? 9.530   8.237   55.387  1.00 19.01 ? 334 SER B C   1 
ATOM   4863 O  O   . SER B 1 334 ? 9.760   9.412   55.311  1.00 21.11 ? 334 SER B O   1 
ATOM   4864 C  CB  . SER B 1 334 ? 11.855  7.405   54.959  1.00 20.71 ? 334 SER B CB  1 
ATOM   4865 O  OG  . SER B 1 334 ? 12.854  6.489   55.332  1.00 22.30 ? 334 SER B OG  1 
ATOM   4866 N  N   . ASN B 1 335 ? 8.339   7.729   55.022  1.00 16.14 ? 335 ASN B N   1 
ATOM   4867 C  CA  . ASN B 1 335 ? 7.297   8.501   54.360  1.00 17.57 ? 335 ASN B CA  1 
ATOM   4868 C  C   . ASN B 1 335 ? 5.944   8.271   55.052  1.00 18.48 ? 335 ASN B C   1 
ATOM   4869 O  O   . ASN B 1 335 ? 4.914   8.294   54.360  1.00 19.31 ? 335 ASN B O   1 
ATOM   4870 C  CB  . ASN B 1 335 ? 7.166   8.162   52.898  1.00 18.61 ? 335 ASN B CB  1 
ATOM   4871 C  CG  . ASN B 1 335 ? 8.405   8.624   52.148  1.00 18.63 ? 335 ASN B CG  1 
ATOM   4872 O  OD1 . ASN B 1 335 ? 8.559   9.827   51.939  1.00 18.94 ? 335 ASN B OD1 1 
ATOM   4873 N  ND2 . ASN B 1 335 ? 9.302   7.717   51.831  1.00 16.76 ? 335 ASN B ND2 1 
ATOM   4874 N  N   . GLY B 1 336 ? 5.961   8.033   56.380  1.00 18.81 ? 336 GLY B N   1 
ATOM   4875 C  CA  . GLY B 1 336 ? 4.689   7.929   57.079  1.00 21.68 ? 336 GLY B CA  1 
ATOM   4876 C  C   . GLY B 1 336 ? 3.837   6.726   56.629  1.00 23.81 ? 336 GLY B C   1 
ATOM   4877 O  O   . GLY B 1 336 ? 2.606   6.739   56.753  1.00 24.96 ? 336 GLY B O   1 
ATOM   4878 N  N   . GLY B 1 337 ? 4.482   5.694   56.064  1.00 19.69 ? 337 GLY B N   1 
ATOM   4879 C  CA  . GLY B 1 337 ? 3.794   4.482   55.624  1.00 21.76 ? 337 GLY B CA  1 
ATOM   4880 C  C   . GLY B 1 337 ? 3.367   4.504   54.139  1.00 20.35 ? 337 GLY B C   1 
ATOM   4881 O  O   . GLY B 1 337 ? 2.815   3.483   53.655  1.00 18.45 ? 337 GLY B O   1 
ATOM   4882 N  N   . ALA B 1 338 ? 3.665   5.586   53.426  1.00 18.51 ? 338 ALA B N   1 
ATOM   4883 C  CA  . ALA B 1 338 ? 3.208   5.744   52.028  1.00 20.02 ? 338 ALA B CA  1 
ATOM   4884 C  C   . ALA B 1 338 ? 3.859   4.643   51.181  1.00 17.67 ? 338 ALA B C   1 
ATOM   4885 O  O   . ALA B 1 338 ? 5.086   4.514   51.198  1.00 17.26 ? 338 ALA B O   1 
ATOM   4886 C  CB  . ALA B 1 338 ? 3.605   7.083   51.482  1.00 21.62 ? 338 ALA B CB  1 
ATOM   4887 N  N   . THR B 1 339 ? 3.064   3.907   50.393  1.00 17.56 ? 339 THR B N   1 
ATOM   4888 C  CA  . THR B 1 339 ? 3.535   2.749   49.658  1.00 19.15 ? 339 THR B CA  1 
ATOM   4889 C  C   . THR B 1 339 ? 2.899   2.857   48.261  1.00 16.71 ? 339 THR B C   1 
ATOM   4890 O  O   . THR B 1 339 ? 1.753   3.229   48.138  1.00 19.07 ? 339 THR B O   1 
ATOM   4891 C  CB  . THR B 1 339 ? 3.131   1.418   50.336  1.00 20.02 ? 339 THR B CB  1 
ATOM   4892 O  OG1 . THR B 1 339 ? 3.530   1.478   51.724  1.00 22.76 ? 339 THR B OG1 1 
ATOM   4893 C  CG2 . THR B 1 339 ? 3.752   0.206   49.698  1.00 19.53 ? 339 THR B CG2 1 
ATOM   4894 N  N   . LEU B 1 340 ? 3.655   2.433   47.244  1.00 16.23 ? 340 LEU B N   1 
ATOM   4895 C  CA  . LEU B 1 340 ? 3.297   2.606   45.840  1.00 17.10 ? 340 LEU B CA  1 
ATOM   4896 C  C   . LEU B 1 340 ? 3.300   1.251   45.153  1.00 14.35 ? 340 LEU B C   1 
ATOM   4897 O  O   . LEU B 1 340 ? 4.094   0.403   45.506  1.00 17.16 ? 340 LEU B O   1 
ATOM   4898 C  CB  . LEU B 1 340 ? 4.358   3.493   45.130  1.00 21.65 ? 340 LEU B CB  1 
ATOM   4899 C  CG  . LEU B 1 340 ? 4.557   4.909   45.647  1.00 23.40 ? 340 LEU B CG  1 
ATOM   4900 C  CD1 . LEU B 1 340 ? 5.669   5.589   44.875  1.00 27.72 ? 340 LEU B CD1 1 
ATOM   4901 C  CD2 . LEU B 1 340 ? 3.260   5.699   45.504  1.00 33.38 ? 340 LEU B CD2 1 
ATOM   4902 N  N   A LEU B 1 341 ? 2.484   1.108   44.095  0.45 13.90 ? 341 LEU B N   1 
ATOM   4903 N  N   B LEU B 1 341 ? 2.492   1.088   44.102  0.55 14.21 ? 341 LEU B N   1 
ATOM   4904 C  CA  A LEU B 1 341 ? 2.667   0.046   43.108  0.45 12.92 ? 341 LEU B CA  1 
ATOM   4905 C  CA  B LEU B 1 341 ? 2.750   0.008   43.160  0.55 13.30 ? 341 LEU B CA  1 
ATOM   4906 C  C   A LEU B 1 341 ? 3.455   0.616   41.927  0.45 13.72 ? 341 LEU B C   1 
ATOM   4907 C  C   B LEU B 1 341 ? 3.463   0.600   41.947  0.55 14.12 ? 341 LEU B C   1 
ATOM   4908 O  O   A LEU B 1 341 ? 2.911   1.411   41.151  0.45 12.92 ? 341 LEU B O   1 
ATOM   4909 O  O   B LEU B 1 341 ? 2.902   1.440   41.225  0.55 12.98 ? 341 LEU B O   1 
ATOM   4910 C  CB  A LEU B 1 341 ? 1.287   -0.455  42.650  0.45 13.16 ? 341 LEU B CB  1 
ATOM   4911 C  CB  B LEU B 1 341 ? 1.433   -0.659  42.759  0.55 14.49 ? 341 LEU B CB  1 
ATOM   4912 C  CG  A LEU B 1 341 ? 1.264   -1.549  41.578  0.45 12.46 ? 341 LEU B CG  1 
ATOM   4913 C  CG  B LEU B 1 341 ? 1.622   -1.965  41.989  0.55 13.72 ? 341 LEU B CG  1 
ATOM   4914 C  CD1 A LEU B 1 341 ? 2.275   -2.628  41.871  0.45 12.70 ? 341 LEU B CD1 1 
ATOM   4915 C  CD1 B LEU B 1 341 ? 0.565   -2.961  42.385  0.55 16.52 ? 341 LEU B CD1 1 
ATOM   4916 C  CD2 A LEU B 1 341 ? -0.121  -2.148  41.461  0.45 12.05 ? 341 LEU B CD2 1 
ATOM   4917 C  CD2 B LEU B 1 341 ? 1.619   -1.712  40.481  0.55 13.28 ? 341 LEU B CD2 1 
ATOM   4918 N  N   . ARG B 1 342 ? 4.731   0.245   41.819  1.00 12.26 ? 342 ARG B N   1 
ATOM   4919 C  CA  . ARG B 1 342 ? 5.533   0.626   40.667  1.00 12.48 ? 342 ARG B CA  1 
ATOM   4920 C  C   . ARG B 1 342 ? 5.338   -0.396  39.544  1.00 12.54 ? 342 ARG B C   1 
ATOM   4921 O  O   . ARG B 1 342 ? 5.306   -1.598  39.800  1.00 14.93 ? 342 ARG B O   1 
ATOM   4922 C  CB  . ARG B 1 342 ? 6.989   0.693   41.065  1.00 13.23 ? 342 ARG B CB  1 
ATOM   4923 C  CG  . ARG B 1 342 ? 7.253   1.860   42.025  1.00 12.91 ? 342 ARG B CG  1 
ATOM   4924 C  CD  . ARG B 1 342 ? 8.674   1.877   42.509  1.00 14.32 ? 342 ARG B CD  1 
ATOM   4925 N  NE  . ARG B 1 342 ? 8.928   0.778   43.434  1.00 14.26 ? 342 ARG B NE  1 
ATOM   4926 C  CZ  . ARG B 1 342 ? 10.062  0.077   43.487  1.00 13.07 ? 342 ARG B CZ  1 
ATOM   4927 N  NH1 . ARG B 1 342 ? 11.084  0.223   42.635  1.00 15.68 ? 342 ARG B NH1 1 
ATOM   4928 N  NH2 . ARG B 1 342 ? 10.108  -0.850  44.411  1.00 13.95 ? 342 ARG B NH2 1 
ATOM   4929 N  N   . ARG B 1 343 ? 5.162   0.134   38.331  1.00 12.21 ? 343 ARG B N   1 
ATOM   4930 C  CA  . ARG B 1 343 ? 4.912   -0.726  37.163  1.00 13.35 ? 343 ARG B CA  1 
ATOM   4931 C  C   . ARG B 1 343 ? 5.564   -0.150  35.919  1.00 13.88 ? 343 ARG B C   1 
ATOM   4932 O  O   . ARG B 1 343 ? 5.020   -0.178  34.842  1.00 15.03 ? 343 ARG B O   1 
ATOM   4933 C  CB  . ARG B 1 343 ? 3.405   -0.902  37.045  1.00 11.88 ? 343 ARG B CB  1 
ATOM   4934 C  CG  . ARG B 1 343 ? 3.059   -2.275  36.490  1.00 13.97 ? 343 ARG B CG  1 
ATOM   4935 C  CD  . ARG B 1 343 ? 1.581   -2.553  36.309  1.00 14.17 ? 343 ARG B CD  1 
ATOM   4936 N  NE  . ARG B 1 343 ? 1.312   -3.910  35.800  1.00 13.65 ? 343 ARG B NE  1 
ATOM   4937 C  CZ  . ARG B 1 343 ? 1.288   -4.319  34.504  1.00 13.58 ? 343 ARG B CZ  1 
ATOM   4938 N  NH1 . ARG B 1 343 ? 1.767   -3.576  33.503  1.00 12.38 ? 343 ARG B NH1 1 
ATOM   4939 N  NH2 . ARG B 1 343 ? 0.826   -5.508  34.193  1.00 13.06 ? 343 ARG B NH2 1 
ATOM   4940 N  N   . GLY B 1 344 ? 6.735   0.474   36.080  1.00 13.07 ? 344 GLY B N   1 
ATOM   4941 C  CA  . GLY B 1 344 ? 7.428   1.138   35.013  1.00 14.22 ? 344 GLY B CA  1 
ATOM   4942 C  C   . GLY B 1 344 ? 8.288   0.179   34.169  1.00 12.94 ? 344 GLY B C   1 
ATOM   4943 O  O   . GLY B 1 344 ? 8.413   -1.035  34.424  1.00 12.57 ? 344 GLY B O   1 
ATOM   4944 N  N   . TYR B 1 345 ? 8.838   0.786   33.136  1.00 14.06 ? 345 TYR B N   1 
ATOM   4945 C  CA  . TYR B 1 345 ? 9.556   0.110   32.063  1.00 12.35 ? 345 TYR B CA  1 
ATOM   4946 C  C   . TYR B 1 345 ? 10.753  0.962   31.717  1.00 12.59 ? 345 TYR B C   1 
ATOM   4947 O  O   . TYR B 1 345 ? 10.713  2.212   31.731  1.00 14.10 ? 345 TYR B O   1 
ATOM   4948 C  CB  . TYR B 1 345 ? 8.657   0.011   30.830  1.00 11.65 ? 345 TYR B CB  1 
ATOM   4949 C  CG  . TYR B 1 345 ? 7.621   -1.064  30.949  1.00 11.26 ? 345 TYR B CG  1 
ATOM   4950 C  CD1 . TYR B 1 345 ? 6.448   -0.879  31.692  1.00 12.88 ? 345 TYR B CD1 1 
ATOM   4951 C  CD2 . TYR B 1 345 ? 7.806   -2.290  30.344  1.00 12.40 ? 345 TYR B CD2 1 
ATOM   4952 C  CE1 . TYR B 1 345 ? 5.503   -1.879  31.764  1.00 12.26 ? 345 TYR B CE1 1 
ATOM   4953 C  CE2 . TYR B 1 345 ? 6.898   -3.316  30.469  1.00 13.56 ? 345 TYR B CE2 1 
ATOM   4954 C  CZ  . TYR B 1 345 ? 5.715   -3.100  31.150  1.00 13.19 ? 345 TYR B CZ  1 
ATOM   4955 O  OH  . TYR B 1 345 ? 4.812   -4.131  31.299  1.00 13.77 ? 345 TYR B OH  1 
ATOM   4956 N  N   . SER B 1 346 ? 11.797  0.281   31.326  1.00 15.34 ? 346 SER B N   1 
ATOM   4957 C  CA  . SER B 1 346 ? 12.940  0.972   30.768  1.00 14.49 ? 346 SER B CA  1 
ATOM   4958 C  C   . SER B 1 346 ? 12.663  1.462   29.347  1.00 16.15 ? 346 SER B C   1 
ATOM   4959 O  O   . SER B 1 346 ? 11.814  0.959   28.626  1.00 17.83 ? 346 SER B O   1 
ATOM   4960 C  CB  . SER B 1 346 ? 14.144  0.043   30.708  1.00 16.80 ? 346 SER B CB  1 
ATOM   4961 O  OG  . SER B 1 346 ? 14.518  -0.390  32.001  1.00 16.97 ? 346 SER B OG  1 
ATOM   4962 N  N   . PHE B 1 347 ? 13.336  2.512   28.962  1.00 15.88 ? 347 PHE B N   1 
ATOM   4963 C  CA  . PHE B 1 347 ? 13.320  2.954   27.597  1.00 15.53 ? 347 PHE B CA  1 
ATOM   4964 C  C   . PHE B 1 347 ? 14.714  3.211   27.101  1.00 18.46 ? 347 PHE B C   1 
ATOM   4965 O  O   . PHE B 1 347 ? 15.603  3.670   27.822  1.00 18.78 ? 347 PHE B O   1 
ATOM   4966 C  CB  . PHE B 1 347 ? 12.394  4.164   27.409  1.00 17.14 ? 347 PHE B CB  1 
ATOM   4967 C  CG  . PHE B 1 347 ? 12.904  5.483   27.944  1.00 15.11 ? 347 PHE B CG  1 
ATOM   4968 C  CD1 . PHE B 1 347 ? 13.743  6.331   27.223  1.00 16.68 ? 347 PHE B CD1 1 
ATOM   4969 C  CD2 . PHE B 1 347 ? 12.462  5.896   29.190  1.00 18.50 ? 347 PHE B CD2 1 
ATOM   4970 C  CE1 . PHE B 1 347 ? 14.215  7.512   27.759  1.00 16.34 ? 347 PHE B CE1 1 
ATOM   4971 C  CE2 . PHE B 1 347 ? 12.920  7.096   29.718  1.00 16.30 ? 347 PHE B CE2 1 
ATOM   4972 C  CZ  . PHE B 1 347 ? 13.782  7.901   28.994  1.00 18.43 ? 347 PHE B CZ  1 
ATOM   4973 N  N   . THR B 1 348 ? 14.832  3.071   25.779  1.00 17.97 ? 348 THR B N   1 
ATOM   4974 C  CA  . THR B 1 348 ? 15.999  3.582   25.099  1.00 18.44 ? 348 THR B CA  1 
ATOM   4975 C  C   . THR B 1 348 ? 15.504  4.016   23.750  1.00 21.16 ? 348 THR B C   1 
ATOM   4976 O  O   . THR B 1 348 ? 15.067  3.153   22.990  1.00 21.09 ? 348 THR B O   1 
ATOM   4977 C  CB  . THR B 1 348 ? 17.099  2.533   24.919  1.00 20.65 ? 348 THR B CB  1 
ATOM   4978 O  OG1 . THR B 1 348 ? 17.499  1.989   26.196  1.00 24.79 ? 348 THR B OG1 1 
ATOM   4979 C  CG2 . THR B 1 348 ? 18.263  3.130   24.142  1.00 21.10 ? 348 THR B CG2 1 
ATOM   4980 N  N   . ASP B 1 349 ? 15.604  5.303   23.501  1.00 17.97 ? 349 ASP B N   1 
ATOM   4981 C  CA  . ASP B 1 349 ? 14.957  5.920   22.381  1.00 22.05 ? 349 ASP B CA  1 
ATOM   4982 C  C   . ASP B 1 349 ? 15.945  6.161   21.246  1.00 25.80 ? 349 ASP B C   1 
ATOM   4983 O  O   . ASP B 1 349 ? 15.514  6.260   20.086  1.00 26.13 ? 349 ASP B O   1 
ATOM   4984 C  CB  . ASP B 1 349 ? 14.183  7.153   22.840  1.00 24.92 ? 349 ASP B CB  1 
ATOM   4985 C  CG  . ASP B 1 349 ? 12.868  6.764   23.525  1.00 24.34 ? 349 ASP B CG  1 
ATOM   4986 O  OD1 . ASP B 1 349 ? 12.501  5.546   23.531  1.00 24.56 ? 349 ASP B OD1 1 
ATOM   4987 O  OD2 . ASP B 1 349 ? 12.282  7.639   24.154  1.00 33.25 ? 349 ASP B OD2 1 
ATOM   4988 N  N   . GLY B 1 350 ? 17.250  6.159   21.549  1.00 19.05 ? 350 GLY B N   1 
ATOM   4989 C  CA  . GLY B 1 350 ? 18.220  6.497   20.526  1.00 21.97 ? 350 GLY B CA  1 
ATOM   4990 C  C   . GLY B 1 350 ? 19.319  7.345   21.166  1.00 21.45 ? 350 GLY B C   1 
ATOM   4991 O  O   . GLY B 1 350 ? 19.698  7.106   22.303  1.00 21.60 ? 350 GLY B O   1 
ATOM   4992 N  N   . THR B 1 351 ? 19.932  8.194   20.389  1.00 24.25 ? 351 THR B N   1 
ATOM   4993 C  CA  . THR B 1 351 ? 21.026  8.993   20.947  1.00 21.80 ? 351 THR B CA  1 
ATOM   4994 C  C   . THR B 1 351 ? 20.611  10.406  20.663  1.00 25.55 ? 351 THR B C   1 
ATOM   4995 O  O   . THR B 1 351 ? 19.895  10.643  19.703  1.00 25.28 ? 351 THR B O   1 
ATOM   4996 C  CB  . THR B 1 351 ? 22.423  8.547   20.530  1.00 28.93 ? 351 THR B CB  1 
ATOM   4997 O  OG1 . THR B 1 351 ? 22.289  8.322   19.148  1.00 27.63 ? 351 THR B OG1 1 
ATOM   4998 C  CG2 . THR B 1 351 ? 22.905  7.258   21.197  1.00 30.33 ? 351 THR B CG2 1 
ATOM   4999 N  N   . ASP B 1 352 ? 21.034  11.299  21.549  1.00 29.22 ? 352 ASP B N   1 
ATOM   5000 C  CA  . ASP B 1 352 ? 20.677  12.702  21.439  1.00 34.95 ? 352 ASP B CA  1 
ATOM   5001 C  C   . ASP B 1 352 ? 21.748  13.375  20.586  1.00 32.21 ? 352 ASP B C   1 
ATOM   5002 O  O   . ASP B 1 352 ? 22.607  12.697  20.006  1.00 31.10 ? 352 ASP B O   1 
ATOM   5003 C  CB  . ASP B 1 352 ? 20.521  13.349  22.813  1.00 36.87 ? 352 ASP B CB  1 
ATOM   5004 C  CG  . ASP B 1 352 ? 21.791  13.411  23.649  1.00 27.64 ? 352 ASP B CG  1 
ATOM   5005 O  OD1 . ASP B 1 352 ? 22.898  13.312  23.078  1.00 28.04 ? 352 ASP B OD1 1 
ATOM   5006 O  OD2 . ASP B 1 352 ? 21.646  13.496  24.885  1.00 37.59 ? 352 ASP B OD2 1 
ATOM   5007 N  N   . GLY B 1 353 ? 21.633  14.709  20.482  1.00 38.44 ? 353 GLY B N   1 
ATOM   5008 C  CA  . GLY B 1 353 ? 22.516  15.530  19.666  1.00 40.80 ? 353 GLY B CA  1 
ATOM   5009 C  C   . GLY B 1 353 ? 23.981  15.510  20.101  1.00 41.09 ? 353 GLY B C   1 
ATOM   5010 O  O   . GLY B 1 353 ? 24.851  15.747  19.267  1.00 44.97 ? 353 GLY B O   1 
ATOM   5011 N  N   . LEU B 1 354 ? 24.264  15.161  21.373  1.00 39.81 ? 354 LEU B N   1 
ATOM   5012 C  CA  . LEU B 1 354 ? 25.638  15.111  21.875  1.00 38.55 ? 354 LEU B CA  1 
ATOM   5013 C  C   . LEU B 1 354 ? 26.281  13.730  21.694  1.00 38.89 ? 354 LEU B C   1 
ATOM   5014 O  O   . LEU B 1 354 ? 27.418  13.539  22.074  1.00 39.87 ? 354 LEU B O   1 
ATOM   5015 C  CB  . LEU B 1 354 ? 25.647  15.533  23.346  1.00 47.70 ? 354 LEU B CB  1 
ATOM   5016 C  CG  . LEU B 1 354 ? 24.886  16.823  23.701  1.00 56.30 ? 354 LEU B CG  1 
ATOM   5017 C  CD1 . LEU B 1 354 ? 25.168  17.234  25.143  1.00 59.15 ? 354 LEU B CD1 1 
ATOM   5018 C  CD2 . LEU B 1 354 ? 25.213  17.972  22.752  1.00 55.72 ? 354 LEU B CD2 1 
ATOM   5019 N  N   . GLY B 1 355 ? 25.554  12.732  21.156  1.00 32.21 ? 355 GLY B N   1 
ATOM   5020 C  CA  . GLY B 1 355 ? 26.080  11.377  21.043  1.00 33.80 ? 355 GLY B CA  1 
ATOM   5021 C  C   . GLY B 1 355 ? 25.822  10.541  22.302  1.00 25.50 ? 355 GLY B C   1 
ATOM   5022 O  O   . GLY B 1 355 ? 26.264  9.409   22.391  1.00 31.21 ? 355 GLY B O   1 
ATOM   5023 N  N   . ARG B 1 356 ? 25.000  11.066  23.216  1.00 23.59 ? 356 ARG B N   1 
ATOM   5024 C  CA  . ARG B 1 356 ? 24.680  10.444  24.504  1.00 24.50 ? 356 ARG B CA  1 
ATOM   5025 C  C   . ARG B 1 356 ? 23.457  9.535   24.350  1.00 24.78 ? 356 ARG B C   1 
ATOM   5026 O  O   . ARG B 1 356 ? 22.558  9.817   23.555  1.00 22.79 ? 356 ARG B O   1 
ATOM   5027 C  CB  . ARG B 1 356 ? 24.360  11.526  25.548  1.00 29.52 ? 356 ARG B CB  1 
ATOM   5028 C  CG  . ARG B 1 356 ? 25.585  12.265  26.100  1.00 30.21 ? 356 ARG B CG  1 
ATOM   5029 C  CD  . ARG B 1 356 ? 25.142  13.331  27.085  1.00 38.06 ? 356 ARG B CD  1 
ATOM   5030 N  N   . LEU B 1 357 ? 23.304  8.559   25.242  1.00 22.48 ? 357 LEU B N   1 
ATOM   5031 C  CA  . LEU B 1 357 ? 22.227  7.599   25.095  1.00 23.95 ? 357 LEU B CA  1 
ATOM   5032 C  C   . LEU B 1 357 ? 20.971  8.215   25.712  1.00 25.41 ? 357 LEU B C   1 
ATOM   5033 O  O   . LEU B 1 357 ? 20.981  8.573   26.894  1.00 24.25 ? 357 LEU B O   1 
ATOM   5034 C  CB  . LEU B 1 357 ? 22.715  6.323   25.819  1.00 29.42 ? 357 LEU B CB  1 
ATOM   5035 C  CG  . LEU B 1 357 ? 22.341  4.942   25.292  1.00 37.16 ? 357 LEU B CG  1 
ATOM   5036 C  CD1 . LEU B 1 357 ? 22.871  4.675   23.899  1.00 38.16 ? 357 LEU B CD1 1 
ATOM   5037 C  CD2 . LEU B 1 357 ? 22.897  3.900   26.264  1.00 38.98 ? 357 LEU B CD2 1 
ATOM   5038 N  N   . ASP B 1 358 ? 19.908  8.306   24.913  1.00 18.73 ? 358 ASP B N   1 
ATOM   5039 C  CA  . ASP B 1 358 ? 18.624  8.769   25.377  1.00 20.87 ? 358 ASP B CA  1 
ATOM   5040 C  C   . ASP B 1 358 ? 17.891  7.566   25.937  1.00 21.71 ? 358 ASP B C   1 
ATOM   5041 O  O   . ASP B 1 358 ? 17.202  6.811   25.217  1.00 19.52 ? 358 ASP B O   1 
ATOM   5042 C  CB  . ASP B 1 358 ? 17.867  9.450   24.239  1.00 23.34 ? 358 ASP B CB  1 
ATOM   5043 C  CG  . ASP B 1 358 ? 16.549  10.088  24.657  1.00 25.16 ? 358 ASP B CG  1 
ATOM   5044 O  OD1 . ASP B 1 358 ? 16.177  9.961   25.821  1.00 24.05 ? 358 ASP B OD1 1 
ATOM   5045 O  OD2 . ASP B 1 358 ? 15.860  10.679  23.784  1.00 28.86 ? 358 ASP B OD2 1 
ATOM   5046 N  N   . ALA B 1 359 ? 18.095  7.366   27.230  1.00 17.88 ? 359 ALA B N   1 
ATOM   5047 C  CA  . ALA B 1 359 ? 17.671  6.152   27.903  1.00 16.26 ? 359 ALA B CA  1 
ATOM   5048 C  C   . ALA B 1 359 ? 17.221  6.539   29.293  1.00 15.16 ? 359 ALA B C   1 
ATOM   5049 O  O   . ALA B 1 359 ? 17.710  7.530   29.827  1.00 14.58 ? 359 ALA B O   1 
ATOM   5050 C  CB  . ALA B 1 359 ? 18.780  5.174   27.922  1.00 16.94 ? 359 ALA B CB  1 
ATOM   5051 N  N   . GLY B 1 360 ? 16.454  5.677   29.894  1.00 15.54 ? 360 GLY B N   1 
ATOM   5052 C  CA  . GLY B 1 360 ? 15.975  5.937   31.244  1.00 16.84 ? 360 GLY B CA  1 
ATOM   5053 C  C   . GLY B 1 360 ? 14.872  4.981   31.658  1.00 17.41 ? 360 GLY B C   1 
ATOM   5054 O  O   . GLY B 1 360 ? 14.870  3.809   31.266  1.00 14.67 ? 360 GLY B O   1 
ATOM   5055 N  N   . LEU B 1 361 ? 14.060  5.496   32.572  1.00 16.04 ? 361 LEU B N   1 
ATOM   5056 C  CA  . LEU B 1 361 ? 12.986  4.739   33.220  1.00 15.88 ? 361 LEU B CA  1 
ATOM   5057 C  C   . LEU B 1 361 ? 11.717  5.530   32.971  1.00 14.10 ? 361 LEU B C   1 
ATOM   5058 O  O   . LEU B 1 361 ? 11.641  6.733   33.251  1.00 14.15 ? 361 LEU B O   1 
ATOM   5059 C  CB  . LEU B 1 361 ? 13.209  4.498   34.716  1.00 17.91 ? 361 LEU B CB  1 
ATOM   5060 C  CG  . LEU B 1 361 ? 12.034  3.847   35.483  1.00 21.79 ? 361 LEU B CG  1 
ATOM   5061 C  CD1 . LEU B 1 361 ? 11.920  2.377   35.163  1.00 26.93 ? 361 LEU B CD1 1 
ATOM   5062 C  CD2 . LEU B 1 361 ? 12.174  4.026   36.988  1.00 28.40 ? 361 LEU B CD2 1 
ATOM   5063 N  N   . PHE B 1 362 ? 10.774  4.880   32.234  1.00 11.87 ? 362 PHE B N   1 
ATOM   5064 C  CA  . PHE B 1 362 ? 9.436   5.405   32.180  1.00 12.26 ? 362 PHE B CA  1 
ATOM   5065 C  C   . PHE B 1 362 ? 8.692   4.900   33.410  1.00 11.05 ? 362 PHE B C   1 
ATOM   5066 O  O   . PHE B 1 362 ? 8.227   3.774   33.495  1.00 13.29 ? 362 PHE B O   1 
ATOM   5067 C  CB  . PHE B 1 362 ? 8.785   5.007   30.855  1.00 12.67 ? 362 PHE B CB  1 
ATOM   5068 C  CG  . PHE B 1 362 ? 7.441   5.667   30.667  1.00 12.25 ? 362 PHE B CG  1 
ATOM   5069 C  CD1 . PHE B 1 362 ? 7.352   7.018   30.439  1.00 15.44 ? 362 PHE B CD1 1 
ATOM   5070 C  CD2 . PHE B 1 362 ? 6.284   4.908   30.582  1.00 13.15 ? 362 PHE B CD2 1 
ATOM   5071 C  CE1 . PHE B 1 362 ? 6.118   7.622   30.215  1.00 14.44 ? 362 PHE B CE1 1 
ATOM   5072 C  CE2 . PHE B 1 362 ? 5.068   5.514   30.395  1.00 15.98 ? 362 PHE B CE2 1 
ATOM   5073 C  CZ  . PHE B 1 362 ? 4.984   6.885   30.278  1.00 13.35 ? 362 PHE B CZ  1 
ATOM   5074 N  N   . PHE B 1 363 ? 8.708   5.733   34.430  1.00 10.85 ? 363 PHE B N   1 
ATOM   5075 C  CA  . PHE B 1 363 ? 8.225   5.376   35.733  1.00 12.82 ? 363 PHE B CA  1 
ATOM   5076 C  C   . PHE B 1 363 ? 6.688   5.508   35.731  1.00 13.08 ? 363 PHE B C   1 
ATOM   5077 O  O   . PHE B 1 363 ? 6.130   6.556   35.397  1.00 13.11 ? 363 PHE B O   1 
ATOM   5078 C  CB  . PHE B 1 363 ? 8.881   6.343   36.741  1.00 12.38 ? 363 PHE B CB  1 
ATOM   5079 C  CG  . PHE B 1 363 ? 8.466   6.124   38.156  1.00 13.33 ? 363 PHE B CG  1 
ATOM   5080 C  CD1 . PHE B 1 363 ? 7.307   6.697   38.649  1.00 17.00 ? 363 PHE B CD1 1 
ATOM   5081 C  CD2 . PHE B 1 363 ? 9.192   5.257   38.956  1.00 15.75 ? 363 PHE B CD2 1 
ATOM   5082 C  CE1 . PHE B 1 363 ? 6.967   6.469   39.981  1.00 16.48 ? 363 PHE B CE1 1 
ATOM   5083 C  CE2 . PHE B 1 363 ? 8.767   4.988   40.246  1.00 15.58 ? 363 PHE B CE2 1 
ATOM   5084 C  CZ  . PHE B 1 363 ? 7.701   5.637   40.752  1.00 15.58 ? 363 PHE B CZ  1 
ATOM   5085 N  N   . LEU B 1 364 ? 6.016   4.454   36.189  1.00 12.18 ? 364 LEU B N   1 
ATOM   5086 C  CA  . LEU B 1 364 ? 4.594   4.414   36.333  1.00 12.52 ? 364 LEU B CA  1 
ATOM   5087 C  C   . LEU B 1 364 ? 4.314   3.940   37.739  1.00 12.03 ? 364 LEU B C   1 
ATOM   5088 O  O   . LEU B 1 364 ? 4.819   2.919   38.161  1.00 15.86 ? 364 LEU B O   1 
ATOM   5089 C  CB  . LEU B 1 364 ? 3.976   3.412   35.330  1.00 13.43 ? 364 LEU B CB  1 
ATOM   5090 C  CG  . LEU B 1 364 ? 4.129   3.779   33.867  1.00 13.34 ? 364 LEU B CG  1 
ATOM   5091 C  CD1 . LEU B 1 364 ? 3.595   2.647   32.991  1.00 15.41 ? 364 LEU B CD1 1 
ATOM   5092 C  CD2 . LEU B 1 364 ? 3.460   5.078   33.513  1.00 17.74 ? 364 LEU B CD2 1 
ATOM   5093 N  N   . ALA B 1 365 ? 3.552   4.744   38.442  1.00 12.29 ? 365 ALA B N   1 
ATOM   5094 C  CA  . ALA B 1 365 ? 3.117   4.395   39.788  1.00 13.59 ? 365 ALA B CA  1 
ATOM   5095 C  C   . ALA B 1 365 ? 1.592   4.462   39.835  1.00 10.82 ? 365 ALA B C   1 
ATOM   5096 O  O   . ALA B 1 365 ? 0.969   5.462   39.469  1.00 11.13 ? 365 ALA B O   1 
ATOM   5097 C  CB  . ALA B 1 365 ? 3.750   5.321   40.780  1.00 16.46 ? 365 ALA B CB  1 
ATOM   5098 N  N   . TYR B 1 366 ? 1.023   3.430   40.430  1.00 11.06 ? 366 TYR B N   1 
ATOM   5099 C  CA  . TYR B 1 366 ? -0.412  3.377   40.745  1.00 13.28 ? 366 TYR B CA  1 
ATOM   5100 C  C   . TYR B 1 366 ? -0.612  3.544   42.254  1.00 12.78 ? 366 TYR B C   1 
ATOM   5101 O  O   . TYR B 1 366 ? 0.177   3.001   43.043  1.00 14.94 ? 366 TYR B O   1 
ATOM   5102 C  CB  . TYR B 1 366 ? -1.011  2.049   40.258  1.00 11.84 ? 366 TYR B CB  1 
ATOM   5103 C  CG  . TYR B 1 366 ? -1.136  1.900   38.772  1.00 13.76 ? 366 TYR B CG  1 
ATOM   5104 C  CD1 . TYR B 1 366 ? -2.235  2.430   38.091  1.00 13.38 ? 366 TYR B CD1 1 
ATOM   5105 C  CD2 . TYR B 1 366 ? -0.149  1.298   38.005  1.00 15.50 ? 366 TYR B CD2 1 
ATOM   5106 C  CE1 . TYR B 1 366 ? -2.337  2.377   36.723  1.00 13.02 ? 366 TYR B CE1 1 
ATOM   5107 C  CE2 . TYR B 1 366 ? -0.205  1.258   36.601  1.00 13.76 ? 366 TYR B CE2 1 
ATOM   5108 C  CZ  . TYR B 1 366 ? -1.320  1.774   35.966  1.00 15.72 ? 366 TYR B CZ  1 
ATOM   5109 O  OH  . TYR B 1 366 ? -1.545  1.699   34.612  1.00 14.34 ? 366 TYR B OH  1 
ATOM   5110 N  N   . GLN B 1 367 ? -1.657  4.288   42.597  1.00 12.21 ? 367 GLN B N   1 
ATOM   5111 C  CA  . GLN B 1 367 ? -1.939  4.553   43.987  1.00 12.85 ? 367 GLN B CA  1 
ATOM   5112 C  C   . GLN B 1 367 ? -3.421  4.899   44.172  1.00 11.63 ? 367 GLN B C   1 
ATOM   5113 O  O   . GLN B 1 367 ? -4.099  5.441   43.303  1.00 10.94 ? 367 GLN B O   1 
ATOM   5114 C  CB  . GLN B 1 367 ? -1.045  5.672   44.512  1.00 11.89 ? 367 GLN B CB  1 
ATOM   5115 C  CG  . GLN B 1 367 ? -1.202  7.004   43.807  1.00 13.14 ? 367 GLN B CG  1 
ATOM   5116 C  CD  . GLN B 1 367 ? 0.014   7.336   42.962  1.00 14.84 ? 367 GLN B CD  1 
ATOM   5117 O  OE1 . GLN B 1 367 ? 1.030   7.669   43.511  1.00 21.30 ? 367 GLN B OE1 1 
ATOM   5118 N  NE2 . GLN B 1 367 ? -0.024  7.075   41.650  1.00 13.98 ? 367 GLN B NE2 1 
ATOM   5119 N  N   . ARG B 1 368 ? -3.832  4.787   45.443  1.00 11.65 ? 368 ARG B N   1 
ATOM   5120 C  CA  . ARG B 1 368 ? -5.199  5.085   45.843  1.00 13.78 ? 368 ARG B CA  1 
ATOM   5121 C  C   . ARG B 1 368 ? -5.483  6.588   45.851  1.00 13.74 ? 368 ARG B C   1 
ATOM   5122 O  O   . ARG B 1 368 ? -6.623  6.990   45.671  1.00 14.48 ? 368 ARG B O   1 
ATOM   5123 C  CB  . ARG B 1 368 ? -5.422  4.477   47.229  1.00 13.27 ? 368 ARG B CB  1 
ATOM   5124 C  CG  . ARG B 1 368 ? -6.791  4.733   47.820  1.00 14.68 ? 368 ARG B CG  1 
ATOM   5125 C  CD  . ARG B 1 368 ? -6.981  3.794   48.976  1.00 16.65 ? 368 ARG B CD  1 
ATOM   5126 N  NE  . ARG B 1 368 ? -8.234  3.987   49.642  1.00 18.06 ? 368 ARG B NE  1 
ATOM   5127 C  CZ  . ARG B 1 368 ? -8.500  3.465   50.832  1.00 22.24 ? 368 ARG B CZ  1 
ATOM   5128 N  NH1 . ARG B 1 368 ? -7.676  2.568   51.372  1.00 21.59 ? 368 ARG B NH1 1 
ATOM   5129 N  NH2 . ARG B 1 368 ? -9.599  3.872   51.457  1.00 22.46 ? 368 ARG B NH2 1 
ATOM   5130 N  N   . ASP B 1 369 ? -4.448  7.382   46.102  1.00 14.08 ? 369 ASP B N   1 
ATOM   5131 C  CA  . ASP B 1 369 ? -4.556  8.824   46.139  1.00 15.44 ? 369 ASP B CA  1 
ATOM   5132 C  C   . ASP B 1 369 ? -3.187  9.401   45.826  1.00 15.39 ? 369 ASP B C   1 
ATOM   5133 O  O   . ASP B 1 369 ? -2.193  9.060   46.493  1.00 16.33 ? 369 ASP B O   1 
ATOM   5134 C  CB  . ASP B 1 369 ? -5.036  9.262   47.520  1.00 18.14 ? 369 ASP B CB  1 
ATOM   5135 C  CG  . ASP B 1 369 ? -5.444  10.721  47.626  1.00 20.63 ? 369 ASP B CG  1 
ATOM   5136 O  OD1 . ASP B 1 369 ? -4.818  11.598  46.927  1.00 16.41 ? 369 ASP B OD1 1 
ATOM   5137 O  OD2 . ASP B 1 369 ? -6.480  10.985  48.351  1.00 21.03 ? 369 ASP B OD2 1 
ATOM   5138 N  N   . ILE B 1 370 ? -3.134  10.283  44.800  1.00 12.72 ? 370 ILE B N   1 
ATOM   5139 C  CA  . ILE B 1 370 ? -1.836  10.844  44.439  1.00 14.56 ? 370 ILE B CA  1 
ATOM   5140 C  C   . ILE B 1 370 ? -1.241  11.634  45.606  1.00 14.59 ? 370 ILE B C   1 
ATOM   5141 O  O   . ILE B 1 370 ? -0.045  11.671  45.760  1.00 15.19 ? 370 ILE B O   1 
ATOM   5142 C  CB  . ILE B 1 370 ? -1.993  11.669  43.163  1.00 14.91 ? 370 ILE B CB  1 
ATOM   5143 C  CG1 . ILE B 1 370 ? -2.231  10.727  41.975  1.00 16.52 ? 370 ILE B CG1 1 
ATOM   5144 C  CG2 . ILE B 1 370 ? -0.788  12.591  42.944  1.00 17.74 ? 370 ILE B CG2 1 
ATOM   5145 C  CD1 . ILE B 1 370 ? -2.517  11.442  40.689  1.00 17.74 ? 370 ILE B CD1 1 
ATOM   5146 N  N   . ARG B 1 371 ? -2.107  12.303  46.376  1.00 14.51 ? 371 ARG B N   1 
ATOM   5147 C  CA  . ARG B 1 371 ? -1.608  13.136  47.466  1.00 16.33 ? 371 ARG B CA  1 
ATOM   5148 C  C   . ARG B 1 371 ? -0.888  12.335  48.555  1.00 16.71 ? 371 ARG B C   1 
ATOM   5149 O  O   . ARG B 1 371 ? -0.137  12.925  49.360  1.00 17.70 ? 371 ARG B O   1 
ATOM   5150 C  CB  . ARG B 1 371 ? -2.816  13.870  48.055  1.00 18.03 ? 371 ARG B CB  1 
ATOM   5151 C  CG  . ARG B 1 371 ? -3.462  14.818  47.048  1.00 18.41 ? 371 ARG B CG  1 
ATOM   5152 C  CD  . ARG B 1 371 ? -4.721  15.414  47.558  1.00 20.28 ? 371 ARG B CD  1 
ATOM   5153 N  NE  . ARG B 1 371 ? -5.698  14.386  47.658  1.00 19.42 ? 371 ARG B NE  1 
ATOM   5154 C  CZ  . ARG B 1 371 ? -6.877  14.567  48.206  1.00 23.66 ? 371 ARG B CZ  1 
ATOM   5155 N  NH1 . ARG B 1 371 ? -7.316  15.804  48.462  1.00 22.31 ? 371 ARG B NH1 1 
ATOM   5156 N  NH2 . ARG B 1 371 ? -7.629  13.537  48.431  1.00 20.43 ? 371 ARG B NH2 1 
ATOM   5157 N  N   . THR B 1 372 ? -1.209  11.047  48.708  1.00 16.65 ? 372 THR B N   1 
ATOM   5158 C  CA  . THR B 1 372 ? -0.699  10.193  49.771  1.00 17.28 ? 372 THR B CA  1 
ATOM   5159 C  C   . THR B 1 372 ? 0.185   9.053   49.254  1.00 16.82 ? 372 THR B C   1 
ATOM   5160 O  O   . THR B 1 372 ? 0.651   8.209   50.030  1.00 18.12 ? 372 THR B O   1 
ATOM   5161 C  CB  . THR B 1 372 ? -1.791  9.515   50.588  1.00 19.52 ? 372 THR B CB  1 
ATOM   5162 O  OG1 . THR B 1 372 ? -2.577  8.603   49.789  1.00 18.90 ? 372 THR B OG1 1 
ATOM   5163 C  CG2 . THR B 1 372 ? -2.684  10.542  51.262  1.00 28.87 ? 372 THR B CG2 1 
ATOM   5164 N  N   . GLY B 1 373 ? 0.424   9.032   47.940  1.00 17.42 ? 373 GLY B N   1 
ATOM   5165 C  CA  . GLY B 1 373 ? 1.310   8.055   47.351  1.00 16.32 ? 373 GLY B CA  1 
ATOM   5166 C  C   . GLY B 1 373 ? 2.519   8.756   46.792  1.00 16.04 ? 373 GLY B C   1 
ATOM   5167 O  O   . GLY B 1 373 ? 3.488   8.961   47.511  1.00 18.14 ? 373 GLY B O   1 
ATOM   5168 N  N   . PHE B 1 374 ? 2.473   9.080   45.481  1.00 16.25 ? 374 PHE B N   1 
ATOM   5169 C  CA  . PHE B 1 374 ? 3.634   9.593   44.776  1.00 14.80 ? 374 PHE B CA  1 
ATOM   5170 C  C   . PHE B 1 374 ? 4.106   10.886  45.399  1.00 13.53 ? 374 PHE B C   1 
ATOM   5171 O  O   . PHE B 1 374 ? 5.316   11.106  45.480  1.00 14.66 ? 374 PHE B O   1 
ATOM   5172 C  CB  . PHE B 1 374 ? 3.319   9.803   43.279  1.00 14.23 ? 374 PHE B CB  1 
ATOM   5173 C  CG  . PHE B 1 374 ? 4.444   10.381  42.490  1.00 14.55 ? 374 PHE B CG  1 
ATOM   5174 C  CD1 . PHE B 1 374 ? 5.481   9.579   42.019  1.00 14.32 ? 374 PHE B CD1 1 
ATOM   5175 C  CD2 . PHE B 1 374 ? 4.498   11.758  42.230  1.00 16.93 ? 374 PHE B CD2 1 
ATOM   5176 C  CE1 . PHE B 1 374 ? 6.505   10.144  41.276  1.00 15.51 ? 374 PHE B CE1 1 
ATOM   5177 C  CE2 . PHE B 1 374 ? 5.536   12.318  41.483  1.00 14.49 ? 374 PHE B CE2 1 
ATOM   5178 C  CZ  . PHE B 1 374 ? 6.560   11.499  41.039  1.00 15.08 ? 374 PHE B CZ  1 
ATOM   5179 N  N   . VAL B 1 375 ? 3.149   11.804  45.755  1.00 14.91 ? 375 VAL B N   1 
ATOM   5180 C  CA  . VAL B 1 375 ? 3.567   13.160  46.134  1.00 14.70 ? 375 VAL B CA  1 
ATOM   5181 C  C   . VAL B 1 375 ? 4.536   13.093  47.329  1.00 15.41 ? 375 VAL B C   1 
ATOM   5182 O  O   . VAL B 1 375 ? 5.653   13.610  47.245  1.00 16.13 ? 375 VAL B O   1 
ATOM   5183 C  CB  . VAL B 1 375 ? 2.434   14.179  46.267  1.00 14.96 ? 375 VAL B CB  1 
ATOM   5184 C  CG1 . VAL B 1 375 ? 2.932   15.465  46.953  1.00 17.68 ? 375 VAL B CG1 1 
ATOM   5185 C  CG2 . VAL B 1 375 ? 1.866   14.485  44.910  1.00 17.75 ? 375 VAL B CG2 1 
ATOM   5186 N  N   . PRO B 1 376 ? 4.164   12.487  48.472  1.00 15.73 ? 376 PRO B N   1 
ATOM   5187 C  CA  . PRO B 1 376 ? 5.061   12.492  49.646  1.00 16.83 ? 376 PRO B CA  1 
ATOM   5188 C  C   . PRO B 1 376 ? 6.383   11.791  49.378  1.00 16.59 ? 376 PRO B C   1 
ATOM   5189 O  O   . PRO B 1 376 ? 7.440   12.294  49.763  1.00 14.91 ? 376 PRO B O   1 
ATOM   5190 C  CB  . PRO B 1 376 ? 4.287   11.815  50.757  1.00 18.77 ? 376 PRO B CB  1 
ATOM   5191 C  CG  . PRO B 1 376 ? 3.071   11.240  50.108  1.00 22.77 ? 376 PRO B CG  1 
ATOM   5192 C  CD  . PRO B 1 376 ? 2.827   11.991  48.805  1.00 19.42 ? 376 PRO B CD  1 
ATOM   5193 N  N   . VAL B 1 377 ? 6.358   10.717  48.581  1.00 14.16 ? 377 VAL B N   1 
ATOM   5194 C  CA  . VAL B 1 377 ? 7.570   9.962   48.356  1.00 13.09 ? 377 VAL B CA  1 
ATOM   5195 C  C   . VAL B 1 377 ? 8.523   10.791  47.496  1.00 13.64 ? 377 VAL B C   1 
ATOM   5196 O  O   . VAL B 1 377 ? 9.722   10.926  47.832  1.00 14.57 ? 377 VAL B O   1 
ATOM   5197 C  CB  . VAL B 1 377 ? 7.313   8.559   47.757  1.00 14.45 ? 377 VAL B CB  1 
ATOM   5198 C  CG1 . VAL B 1 377 ? 8.635   7.842   47.479  1.00 15.53 ? 377 VAL B CG1 1 
ATOM   5199 C  CG2 . VAL B 1 377 ? 6.449   7.719   48.693  1.00 14.12 ? 377 VAL B CG2 1 
ATOM   5200 N  N   . GLN B 1 378 ? 8.009   11.334  46.354  1.00 12.11 ? 378 GLN B N   1 
ATOM   5201 C  CA  . GLN B 1 378 ? 8.873   12.104  45.492  1.00 12.90 ? 378 GLN B CA  1 
ATOM   5202 C  C   . GLN B 1 378 ? 9.367   13.381  46.218  1.00 15.61 ? 378 GLN B C   1 
ATOM   5203 O  O   . GLN B 1 378 ? 10.524  13.784  46.050  1.00 13.15 ? 378 GLN B O   1 
ATOM   5204 C  CB  . GLN B 1 378 ? 8.117   12.483  44.234  1.00 13.84 ? 378 GLN B CB  1 
ATOM   5205 C  CG  . GLN B 1 378 ? 8.889   13.402  43.274  1.00 13.93 ? 378 GLN B CG  1 
ATOM   5206 C  CD  . GLN B 1 378 ? 10.225  12.875  42.777  1.00 17.28 ? 378 GLN B CD  1 
ATOM   5207 O  OE1 . GLN B 1 378 ? 10.397  11.670  42.597  1.00 17.78 ? 378 GLN B OE1 1 
ATOM   5208 N  NE2 . GLN B 1 378 ? 11.188  13.770  42.541  1.00 21.16 ? 378 GLN B NE2 1 
ATOM   5209 N  N   . ARG B 1 379 ? 8.492   14.034  47.005  1.00 13.83 ? 379 ARG B N   1 
ATOM   5210 C  CA  . ARG B 1 379 ? 8.946   15.139  47.849  1.00 16.17 ? 379 ARG B CA  1 
ATOM   5211 C  C   . ARG B 1 379 ? 10.143  14.721  48.723  1.00 14.55 ? 379 ARG B C   1 
ATOM   5212 O  O   . ARG B 1 379 ? 11.141  15.456  48.790  1.00 14.35 ? 379 ARG B O   1 
ATOM   5213 C  CB  . ARG B 1 379 ? 7.825   15.622  48.763  1.00 19.54 ? 379 ARG B CB  1 
ATOM   5214 C  CG  . ARG B 1 379 ? 8.252   16.811  49.603  1.00 28.15 ? 379 ARG B CG  1 
ATOM   5215 C  CD  . ARG B 1 379 ? 7.017   17.514  50.117  1.00 38.32 ? 379 ARG B CD  1 
ATOM   5216 N  NE  . ARG B 1 379 ? 6.449   18.392  49.101  1.00 43.41 ? 379 ARG B NE  1 
ATOM   5217 C  CZ  . ARG B 1 379 ? 5.147   18.498  48.814  1.00 50.93 ? 379 ARG B CZ  1 
ATOM   5218 N  NH1 . ARG B 1 379 ? 4.217   17.927  49.578  1.00 43.75 ? 379 ARG B NH1 1 
ATOM   5219 N  NH2 . ARG B 1 379 ? 4.782   19.201  47.754  1.00 51.59 ? 379 ARG B NH2 1 
ATOM   5220 N  N   . ASN B 1 380 ? 10.129  13.514  49.316  1.00 12.68 ? 380 ASN B N   1 
ATOM   5221 C  CA  . ASN B 1 380 ? 11.247  13.066  50.152  1.00 14.89 ? 380 ASN B CA  1 
ATOM   5222 C  C   . ASN B 1 380 ? 12.544  12.813  49.355  1.00 15.26 ? 380 ASN B C   1 
ATOM   5223 O  O   . ASN B 1 380 ? 13.633  12.639  49.901  1.00 16.12 ? 380 ASN B O   1 
ATOM   5224 C  CB  . ASN B 1 380 ? 10.813  11.854  50.951  1.00 17.68 ? 380 ASN B CB  1 
ATOM   5225 C  CG  . ASN B 1 380 ? 11.431  11.808  52.321  1.00 19.19 ? 380 ASN B CG  1 
ATOM   5226 O  OD1 . ASN B 1 380 ? 11.554  12.879  52.939  1.00 21.42 ? 380 ASN B OD1 1 
ATOM   5227 N  ND2 . ASN B 1 380 ? 11.976  10.652  52.645  1.00 16.00 ? 380 ASN B ND2 1 
ATOM   5228 N  N   . LEU B 1 381 ? 12.445  12.645  48.020  1.00 14.07 ? 381 LEU B N   1 
ATOM   5229 C  CA  . LEU B 1 381 ? 13.631  12.441  47.200  1.00 12.26 ? 381 LEU B CA  1 
ATOM   5230 C  C   . LEU B 1 381 ? 14.344  13.762  46.856  1.00 14.95 ? 381 LEU B C   1 
ATOM   5231 O  O   . LEU B 1 381 ? 15.174  13.783  45.983  1.00 14.06 ? 381 LEU B O   1 
ATOM   5232 C  CB  . LEU B 1 381 ? 13.227  11.663  45.926  1.00 13.92 ? 381 LEU B CB  1 
ATOM   5233 C  CG  . LEU B 1 381 ? 12.585  10.299  46.148  1.00 14.79 ? 381 LEU B CG  1 
ATOM   5234 C  CD1 . LEU B 1 381 ? 12.339  9.553   44.835  1.00 15.45 ? 381 LEU B CD1 1 
ATOM   5235 C  CD2 . LEU B 1 381 ? 13.486  9.430   46.995  1.00 15.49 ? 381 LEU B CD2 1 
ATOM   5236 N  N   . ALA B 1 382 ? 13.960  14.897  47.470  1.00 15.02 ? 382 ALA B N   1 
ATOM   5237 C  CA  . ALA B 1 382 ? 14.555  16.193  47.203  1.00 17.58 ? 382 ALA B CA  1 
ATOM   5238 C  C   . ALA B 1 382 ? 16.086  16.116  47.284  1.00 18.40 ? 382 ALA B C   1 
ATOM   5239 O  O   . ALA B 1 382 ? 16.765  16.826  46.528  1.00 17.17 ? 382 ALA B O   1 
ATOM   5240 C  CB  . ALA B 1 382 ? 13.970  17.227  48.153  1.00 18.87 ? 382 ALA B CB  1 
ATOM   5241 N  N   . THR B 1 383 ? 16.606  15.291  48.204  1.00 14.85 ? 383 THR B N   1 
ATOM   5242 C  CA  . THR B 1 383 ? 18.030  15.219  48.500  1.00 17.18 ? 383 THR B CA  1 
ATOM   5243 C  C   . THR B 1 383 ? 18.637  13.882  48.062  1.00 16.35 ? 383 THR B C   1 
ATOM   5244 O  O   . THR B 1 383 ? 19.762  13.556  48.405  1.00 15.99 ? 383 THR B O   1 
ATOM   5245 C  CB  . THR B 1 383 ? 18.303  15.465  49.990  1.00 16.79 ? 383 THR B CB  1 
ATOM   5246 O  OG1 . THR B 1 383 ? 17.661  14.495  50.827  1.00 19.50 ? 383 THR B OG1 1 
ATOM   5247 C  CG2 . THR B 1 383 ? 17.857  16.859  50.359  1.00 18.32 ? 383 THR B CG2 1 
ATOM   5248 N  N   . ASP B 1 384 ? 17.895  13.109  47.284  1.00 13.69 ? 384 ASP B N   1 
ATOM   5249 C  CA  . ASP B 1 384 ? 18.352  11.802  46.883  1.00 13.66 ? 384 ASP B CA  1 
ATOM   5250 C  C   . ASP B 1 384 ? 19.698  11.920  46.174  1.00 12.75 ? 384 ASP B C   1 
ATOM   5251 O  O   . ASP B 1 384 ? 19.843  12.660  45.227  1.00 14.23 ? 384 ASP B O   1 
ATOM   5252 C  CB  . ASP B 1 384 ? 17.262  11.193  45.989  1.00 15.58 ? 384 ASP B CB  1 
ATOM   5253 C  CG  . ASP B 1 384 ? 17.370  9.742   45.570  1.00 16.03 ? 384 ASP B CG  1 
ATOM   5254 O  OD1 . ASP B 1 384 ? 18.368  9.067   45.892  1.00 16.21 ? 384 ASP B OD1 1 
ATOM   5255 O  OD2 . ASP B 1 384 ? 16.392  9.292   44.897  1.00 17.10 ? 384 ASP B OD2 1 
ATOM   5256 N  N   . ALA B 1 385 ? 20.629  11.043  46.571  1.00 13.76 ? 385 ALA B N   1 
ATOM   5257 C  CA  . ALA B 1 385 ? 21.903  10.840  45.921  1.00 16.70 ? 385 ALA B CA  1 
ATOM   5258 C  C   . ALA B 1 385 ? 21.732  10.434  44.456  1.00 15.15 ? 385 ALA B C   1 
ATOM   5259 O  O   . ALA B 1 385 ? 22.574  10.766  43.623  1.00 16.43 ? 385 ALA B O   1 
ATOM   5260 C  CB  . ALA B 1 385 ? 22.765  9.851   46.690  1.00 18.34 ? 385 ALA B CB  1 
ATOM   5261 N  N   . LEU B 1 386 ? 20.592  9.841   44.083  1.00 15.03 ? 386 LEU B N   1 
ATOM   5262 C  CA  . LEU B 1 386 ? 20.359  9.481   42.680  1.00 13.76 ? 386 LEU B CA  1 
ATOM   5263 C  C   . LEU B 1 386 ? 20.134  10.714  41.788  1.00 14.66 ? 386 LEU B C   1 
ATOM   5264 O  O   . LEU B 1 386 ? 20.287  10.631  40.585  1.00 13.86 ? 386 LEU B O   1 
ATOM   5265 C  CB  . LEU B 1 386 ? 19.108  8.587   42.672  1.00 14.24 ? 386 LEU B CB  1 
ATOM   5266 C  CG  . LEU B 1 386 ? 18.679  8.051   41.304  1.00 16.41 ? 386 LEU B CG  1 
ATOM   5267 C  CD1 . LEU B 1 386 ? 19.756  7.176   40.761  1.00 16.33 ? 386 LEU B CD1 1 
ATOM   5268 C  CD2 . LEU B 1 386 ? 17.390  7.251   41.462  1.00 18.63 ? 386 LEU B CD2 1 
ATOM   5269 N  N   . ASN B 1 387 ? 19.745  11.857  42.357  1.00 12.63 ? 387 ASN B N   1 
ATOM   5270 C  CA  . ASN B 1 387 ? 19.372  13.023  41.560  1.00 13.67 ? 387 ASN B CA  1 
ATOM   5271 C  C   . ASN B 1 387 ? 20.509  13.503  40.662  1.00 13.63 ? 387 ASN B C   1 
ATOM   5272 O  O   . ASN B 1 387 ? 20.265  14.082  39.634  1.00 16.12 ? 387 ASN B O   1 
ATOM   5273 C  CB  . ASN B 1 387 ? 18.895  14.182  42.427  1.00 15.83 ? 387 ASN B CB  1 
ATOM   5274 C  CG  . ASN B 1 387 ? 17.547  13.901  43.070  1.00 17.54 ? 387 ASN B CG  1 
ATOM   5275 O  OD1 . ASN B 1 387 ? 16.769  13.160  42.493  1.00 18.07 ? 387 ASN B OD1 1 
ATOM   5276 N  ND2 . ASN B 1 387 ? 17.219  14.591  44.140  1.00 17.61 ? 387 ASN B ND2 1 
ATOM   5277 N  N   . GLU B 1 388 ? 21.758  13.199  41.033  1.00 16.01 ? 388 GLU B N   1 
ATOM   5278 C  CA  . GLU B 1 388 ? 22.926  13.569  40.235  1.00 18.21 ? 388 GLU B CA  1 
ATOM   5279 C  C   . GLU B 1 388 ? 22.875  12.916  38.859  1.00 17.68 ? 388 GLU B C   1 
ATOM   5280 O  O   . GLU B 1 388 ? 23.453  13.446  37.880  1.00 17.48 ? 388 GLU B O   1 
ATOM   5281 C  CB  . GLU B 1 388 ? 24.161  13.165  41.031  1.00 20.18 ? 388 GLU B CB  1 
ATOM   5282 C  CG  . GLU B 1 388 ? 25.450  13.497  40.313  1.00 22.99 ? 388 GLU B CG  1 
ATOM   5283 C  CD  . GLU B 1 388 ? 26.741  13.228  41.096  1.00 30.98 ? 388 GLU B CD  1 
ATOM   5284 O  OE1 . GLU B 1 388 ? 26.687  12.946  42.304  1.00 31.72 ? 388 GLU B OE1 1 
ATOM   5285 O  OE2 . GLU B 1 388 ? 27.820  13.289  40.466  1.00 41.99 ? 388 GLU B OE2 1 
ATOM   5286 N  N   . PHE B 1 389 ? 22.120  11.798  38.773  1.00 12.75 ? 389 PHE B N   1 
ATOM   5287 C  CA  . PHE B 1 389 ? 22.248  10.944  37.598  1.00 16.07 ? 389 PHE B CA  1 
ATOM   5288 C  C   . PHE B 1 389 ? 20.954  10.826  36.809  1.00 17.98 ? 389 PHE B C   1 
ATOM   5289 O  O   . PHE B 1 389 ? 20.969  10.079  35.836  1.00 17.54 ? 389 PHE B O   1 
ATOM   5290 C  CB  . PHE B 1 389 ? 22.672  9.542   37.998  1.00 14.95 ? 389 PHE B CB  1 
ATOM   5291 C  CG  . PHE B 1 389 ? 23.979  9.534   38.742  1.00 14.90 ? 389 PHE B CG  1 
ATOM   5292 C  CD1 . PHE B 1 389 ? 25.161  9.702   38.061  1.00 16.43 ? 389 PHE B CD1 1 
ATOM   5293 C  CD2 . PHE B 1 389 ? 24.002  9.348   40.122  1.00 16.03 ? 389 PHE B CD2 1 
ATOM   5294 C  CE1 . PHE B 1 389 ? 26.377  9.677   38.733  1.00 17.27 ? 389 PHE B CE1 1 
ATOM   5295 C  CE2 . PHE B 1 389 ? 25.223  9.352   40.799  1.00 18.72 ? 389 PHE B CE2 1 
ATOM   5296 C  CZ  . PHE B 1 389 ? 26.390  9.539   40.102  1.00 16.91 ? 389 PHE B CZ  1 
ATOM   5297 N  N   . ILE B 1 390 ? 19.911  11.543  37.225  1.00 13.78 ? 390 ILE B N   1 
ATOM   5298 C  CA  . ILE B 1 390 ? 18.646  11.418  36.531  1.00 14.06 ? 390 ILE B CA  1 
ATOM   5299 C  C   . ILE B 1 390 ? 18.059  12.819  36.366  1.00 14.55 ? 390 ILE B C   1 
ATOM   5300 O  O   . ILE B 1 390 ? 18.433  13.790  37.037  1.00 15.51 ? 390 ILE B O   1 
ATOM   5301 C  CB  . ILE B 1 390 ? 17.700  10.491  37.320  1.00 14.51 ? 390 ILE B CB  1 
ATOM   5302 C  CG1 . ILE B 1 390 ? 17.286  11.098  38.667  1.00 16.42 ? 390 ILE B CG1 1 
ATOM   5303 C  CG2 . ILE B 1 390 ? 18.260  9.081   37.448  1.00 15.65 ? 390 ILE B CG2 1 
ATOM   5304 C  CD1 . ILE B 1 390 ? 16.043  10.621  39.311  1.00 19.94 ? 390 ILE B CD1 1 
ATOM   5305 N  N   . GLN B 1 391 ? 17.080  12.946  35.492  1.00 13.96 ? 391 GLN B N   1 
ATOM   5306 C  CA  . GLN B 1 391 ? 16.309  14.148  35.356  1.00 14.53 ? 391 GLN B CA  1 
ATOM   5307 C  C   . GLN B 1 391 ? 14.900  13.764  34.908  1.00 14.01 ? 391 GLN B C   1 
ATOM   5308 O  O   . GLN B 1 391 ? 14.735  13.006  33.944  1.00 14.39 ? 391 GLN B O   1 
ATOM   5309 C  CB  . GLN B 1 391 ? 16.961  15.068  34.305  1.00 19.54 ? 391 GLN B CB  1 
ATOM   5310 C  CG  . GLN B 1 391 ? 16.442  16.496  34.417  1.00 23.98 ? 391 GLN B CG  1 
ATOM   5311 C  CD  . GLN B 1 391 ? 17.169  17.410  33.464  1.00 30.78 ? 391 GLN B CD  1 
ATOM   5312 O  OE1 . GLN B 1 391 ? 17.187  17.166  32.268  1.00 26.79 ? 391 GLN B OE1 1 
ATOM   5313 N  NE2 . GLN B 1 391 ? 17.674  18.515  33.978  1.00 35.48 ? 391 GLN B NE2 1 
ATOM   5314 N  N   . HIS B 1 392 ? 13.890  14.293  35.628  1.00 13.31 ? 392 HIS B N   1 
ATOM   5315 C  CA  . HIS B 1 392 ? 12.523  14.092  35.206  1.00 13.60 ? 392 HIS B CA  1 
ATOM   5316 C  C   . HIS B 1 392 ? 12.236  15.058  34.083  1.00 15.13 ? 392 HIS B C   1 
ATOM   5317 O  O   . HIS B 1 392 ? 12.385  16.295  34.286  1.00 14.79 ? 392 HIS B O   1 
ATOM   5318 C  CB  . HIS B 1 392 ? 11.520  14.281  36.341  1.00 16.78 ? 392 HIS B CB  1 
ATOM   5319 C  CG  . HIS B 1 392 ? 11.663  13.334  37.478  1.00 12.84 ? 392 HIS B CG  1 
ATOM   5320 N  ND1 . HIS B 1 392 ? 10.624  12.609  37.915  1.00 13.43 ? 392 HIS B ND1 1 
ATOM   5321 C  CD2 . HIS B 1 392 ? 12.731  13.049  38.272  1.00 15.12 ? 392 HIS B CD2 1 
ATOM   5322 C  CE1 . HIS B 1 392 ? 11.018  11.894  38.947  1.00 14.96 ? 392 HIS B CE1 1 
ATOM   5323 N  NE2 . HIS B 1 392 ? 12.316  12.149  39.190  1.00 15.71 ? 392 HIS B NE2 1 
ATOM   5324 N  N   . VAL B 1 393 ? 11.874  14.472  32.905  1.00 12.15 ? 393 VAL B N   1 
ATOM   5325 C  CA  . VAL B 1 393 ? 11.691  15.297  31.690  1.00 13.89 ? 393 VAL B CA  1 
ATOM   5326 C  C   . VAL B 1 393 ? 10.286  15.186  31.101  1.00 12.64 ? 393 VAL B C   1 
ATOM   5327 O  O   . VAL B 1 393 ? 9.991   15.859  30.130  1.00 14.22 ? 393 VAL B O   1 
ATOM   5328 C  CB  . VAL B 1 393 ? 12.739  14.962  30.622  1.00 14.77 ? 393 VAL B CB  1 
ATOM   5329 C  CG1 . VAL B 1 393 ? 14.145  15.338  31.156  1.00 15.15 ? 393 VAL B CG1 1 
ATOM   5330 C  CG2 . VAL B 1 393 ? 12.586  13.539  30.107  1.00 15.32 ? 393 VAL B CG2 1 
ATOM   5331 N  N   . GLY B 1 394 ? 9.390   14.392  31.732  1.00 12.57 ? 394 GLY B N   1 
ATOM   5332 C  CA  . GLY B 1 394 ? 8.009   14.410  31.279  1.00 12.09 ? 394 GLY B CA  1 
ATOM   5333 C  C   . GLY B 1 394 ? 7.153   13.913  32.411  1.00 14.23 ? 394 GLY B C   1 
ATOM   5334 O  O   . GLY B 1 394 ? 7.672   13.169  33.275  1.00 14.36 ? 394 GLY B O   1 
ATOM   5335 N  N   . SER B 1 395 ? 5.899   14.355  32.438  1.00 12.81 ? 395 SER B N   1 
ATOM   5336 C  CA  . SER B 1 395 ? 5.070   14.025  33.590  1.00 12.05 ? 395 SER B CA  1 
ATOM   5337 C  C   . SER B 1 395 ? 3.604   14.005  33.150  1.00 13.04 ? 395 SER B C   1 
ATOM   5338 O  O   . SER B 1 395 ? 3.166   14.857  32.378  1.00 14.59 ? 395 SER B O   1 
ATOM   5339 C  CB  . SER B 1 395 ? 5.312   15.036  34.696  1.00 15.50 ? 395 SER B CB  1 
ATOM   5340 O  OG  . SER B 1 395 ? 4.480   14.800  35.816  1.00 13.70 ? 395 SER B OG  1 
ATOM   5341 N  N   . ALA B 1 396 ? 2.787   13.132  33.781  1.00 12.93 ? 396 ALA B N   1 
ATOM   5342 C  CA  . ALA B 1 396 ? 1.337   13.241  33.568  1.00 13.04 ? 396 ALA B CA  1 
ATOM   5343 C  C   . ALA B 1 396 ? 0.658   12.428  34.647  1.00 13.70 ? 396 ALA B C   1 
ATOM   5344 O  O   . ALA B 1 396 ? 1.261   11.528  35.208  1.00 13.81 ? 396 ALA B O   1 
ATOM   5345 C  CB  . ALA B 1 396 ? 0.908   12.747  32.192  1.00 14.75 ? 396 ALA B CB  1 
ATOM   5346 N  N   . VAL B 1 397 ? -0.564  12.787  34.968  1.00 12.03 ? 397 VAL B N   1 
ATOM   5347 C  CA  . VAL B 1 397 ? -1.349  12.083  35.955  1.00 12.19 ? 397 VAL B CA  1 
ATOM   5348 C  C   . VAL B 1 397 ? -2.695  11.760  35.326  1.00 12.33 ? 397 VAL B C   1 
ATOM   5349 O  O   . VAL B 1 397 ? -3.211  12.506  34.496  1.00 11.33 ? 397 VAL B O   1 
ATOM   5350 C  CB  . VAL B 1 397 ? -1.524  12.877  37.275  1.00 12.81 ? 397 VAL B CB  1 
ATOM   5351 C  CG1 . VAL B 1 397 ? -0.199  13.128  37.993  1.00 15.25 ? 397 VAL B CG1 1 
ATOM   5352 C  CG2 . VAL B 1 397 ? -2.245  14.190  37.043  1.00 16.26 ? 397 VAL B CG2 1 
ATOM   5353 N  N   . PHE B 1 398 ? -3.199  10.595  35.742  1.00 12.06 ? 398 PHE B N   1 
ATOM   5354 C  CA  . PHE B 1 398 ? -4.453  10.125  35.207  1.00 14.09 ? 398 PHE B CA  1 
ATOM   5355 C  C   . PHE B 1 398 ? -5.266  9.410   36.289  1.00 12.72 ? 398 PHE B C   1 
ATOM   5356 O  O   . PHE B 1 398 ? -4.706  8.725   37.171  1.00 13.80 ? 398 PHE B O   1 
ATOM   5357 C  CB  . PHE B 1 398 ? -4.232  9.168   34.045  1.00 12.95 ? 398 PHE B CB  1 
ATOM   5358 C  CG  . PHE B 1 398 ? -3.418  9.675   32.890  1.00 12.73 ? 398 PHE B CG  1 
ATOM   5359 C  CD1 . PHE B 1 398 ? -3.982  10.466  31.928  1.00 13.52 ? 398 PHE B CD1 1 
ATOM   5360 C  CD2 . PHE B 1 398 ? -2.056  9.470   32.884  1.00 14.37 ? 398 PHE B CD2 1 
ATOM   5361 C  CE1 . PHE B 1 398 ? -3.219  10.989  30.899  1.00 12.02 ? 398 PHE B CE1 1 
ATOM   5362 C  CE2 . PHE B 1 398 ? -1.277  10.009  31.864  1.00 12.63 ? 398 PHE B CE2 1 
ATOM   5363 C  CZ  . PHE B 1 398 ? -1.868  10.757  30.871  1.00 13.72 ? 398 PHE B CZ  1 
ATOM   5364 N  N   . ALA B 1 399 ? -6.566  9.568   36.177  1.00 11.15 ? 399 ALA B N   1 
ATOM   5365 C  CA  . ALA B 1 399 ? -7.559  8.755   36.887  1.00 13.60 ? 399 ALA B CA  1 
ATOM   5366 C  C   . ALA B 1 399 ? -7.916  7.567   36.005  1.00 12.32 ? 399 ALA B C   1 
ATOM   5367 O  O   . ALA B 1 399 ? -8.372  7.750   34.888  1.00 12.07 ? 399 ALA B O   1 
ATOM   5368 C  CB  . ALA B 1 399 ? -8.783  9.555   37.244  1.00 13.24 ? 399 ALA B CB  1 
ATOM   5369 N  N   . VAL B 1 400 ? -7.581  6.381   36.504  1.00 12.26 ? 400 VAL B N   1 
ATOM   5370 C  CA  . VAL B 1 400 ? -7.805  5.122   35.801  1.00 12.05 ? 400 VAL B CA  1 
ATOM   5371 C  C   . VAL B 1 400 ? -9.128  4.539   36.299  1.00 12.68 ? 400 VAL B C   1 
ATOM   5372 O  O   . VAL B 1 400 ? -9.236  4.110   37.453  1.00 13.80 ? 400 VAL B O   1 
ATOM   5373 C  CB  . VAL B 1 400 ? -6.633  4.199   36.100  1.00 13.78 ? 400 VAL B CB  1 
ATOM   5374 C  CG1 . VAL B 1 400 ? -6.877  2.818   35.522  1.00 13.67 ? 400 VAL B CG1 1 
ATOM   5375 C  CG2 . VAL B 1 400 ? -5.323  4.832   35.628  1.00 15.43 ? 400 VAL B CG2 1 
ATOM   5376 N  N   . PRO B 1 401 ? -10.184 4.549   35.499  1.00 12.29 ? 401 PRO B N   1 
ATOM   5377 C  CA  . PRO B 1 401 ? -11.483 4.148   36.048  1.00 13.39 ? 401 PRO B CA  1 
ATOM   5378 C  C   . PRO B 1 401 ? -11.554 2.659   36.413  1.00 12.11 ? 401 PRO B C   1 
ATOM   5379 O  O   . PRO B 1 401 ? -10.673 1.845   36.113  1.00 12.43 ? 401 PRO B O   1 
ATOM   5380 C  CB  . PRO B 1 401 ? -12.502 4.520   34.958  1.00 14.31 ? 401 PRO B CB  1 
ATOM   5381 C  CG  . PRO B 1 401 ? -11.673 4.605   33.700  1.00 16.45 ? 401 PRO B CG  1 
ATOM   5382 C  CD  . PRO B 1 401 ? -10.275 5.072   34.144  1.00 14.01 ? 401 PRO B CD  1 
ATOM   5383 N  N   . PRO B 1 402 ? -12.673 2.245   37.015  1.00 13.80 ? 402 PRO B N   1 
ATOM   5384 C  CA  . PRO B 1 402 ? -12.922 0.833   37.334  1.00 13.61 ? 402 PRO B CA  1 
ATOM   5385 C  C   . PRO B 1 402 ? -12.948 0.008   36.044  1.00 11.80 ? 402 PRO B C   1 
ATOM   5386 O  O   . PRO B 1 402 ? -12.980 0.520   34.919  1.00 12.19 ? 402 PRO B O   1 
ATOM   5387 C  CB  . PRO B 1 402 ? -14.294 0.837   38.066  1.00 16.62 ? 402 PRO B CB  1 
ATOM   5388 C  CG  . PRO B 1 402 ? -14.896 2.182   37.815  1.00 17.61 ? 402 PRO B CG  1 
ATOM   5389 C  CD  . PRO B 1 402 ? -13.729 3.110   37.576  1.00 18.12 ? 402 PRO B CD  1 
ATOM   5390 N  N   . GLY B 1 403 ? -12.978 -1.287  36.262  1.00 13.05 ? 403 GLY B N   1 
ATOM   5391 C  CA  . GLY B 1 403 ? -13.006 -2.219  35.149  1.00 14.02 ? 403 GLY B CA  1 
ATOM   5392 C  C   . GLY B 1 403 ? -14.325 -2.257  34.404  1.00 13.33 ? 403 GLY B C   1 
ATOM   5393 O  O   . GLY B 1 403 ? -15.384 -1.700  34.789  1.00 12.60 ? 403 GLY B O   1 
ATOM   5394 N  N   . VAL B 1 404 ? -14.195 -2.941  33.274  1.00 14.36 ? 404 VAL B N   1 
ATOM   5395 C  CA  . VAL B 1 404 ? -15.307 -3.175  32.388  1.00 14.86 ? 404 VAL B CA  1 
ATOM   5396 C  C   . VAL B 1 404 ? -15.921 -4.495  32.865  1.00 15.82 ? 404 VAL B C   1 
ATOM   5397 O  O   . VAL B 1 404 ? -15.266 -5.530  32.780  1.00 17.57 ? 404 VAL B O   1 
ATOM   5398 C  CB  . VAL B 1 404 ? -14.836 -3.232  30.937  1.00 18.07 ? 404 VAL B CB  1 
ATOM   5399 C  CG1 . VAL B 1 404 ? -15.970 -3.513  29.992  1.00 17.53 ? 404 VAL B CG1 1 
ATOM   5400 C  CG2 . VAL B 1 404 ? -14.091 -1.939  30.546  1.00 20.02 ? 404 VAL B CG2 1 
ATOM   5401 N  N   . ARG B 1 405 ? -17.159 -4.420  33.357  1.00 17.75 ? 405 ARG B N   1 
ATOM   5402 C  CA  . ARG B 1 405 ? -17.691 -5.511  34.169  1.00 19.27 ? 405 ARG B CA  1 
ATOM   5403 C  C   . ARG B 1 405 ? -18.084 -6.718  33.301  1.00 20.33 ? 405 ARG B C   1 
ATOM   5404 O  O   . ARG B 1 405 ? -17.857 -7.868  33.681  1.00 23.84 ? 405 ARG B O   1 
ATOM   5405 C  CB  . ARG B 1 405 ? -18.925 -5.030  34.985  1.00 22.38 ? 405 ARG B CB  1 
ATOM   5406 C  CG  . ARG B 1 405 ? -18.650 -3.934  36.011  1.00 32.31 ? 405 ARG B CG  1 
ATOM   5407 C  CD  . ARG B 1 405 ? -17.345 -4.032  36.816  1.00 36.74 ? 405 ARG B CD  1 
ATOM   5408 N  NE  . ARG B 1 405 ? -17.638 -4.283  38.225  1.00 45.30 ? 405 ARG B NE  1 
ATOM   5409 N  N   . ASP B 1 406 ? -18.571 -6.461  32.100  1.00 19.01 ? 406 ASP B N   1 
ATOM   5410 C  CA  . ASP B 1 406 ? -19.046 -7.526  31.224  1.00 22.64 ? 406 ASP B CA  1 
ATOM   5411 C  C   . ASP B 1 406 ? -19.143 -6.974  29.817  1.00 23.61 ? 406 ASP B C   1 
ATOM   5412 O  O   . ASP B 1 406 ? -18.789 -5.837  29.545  1.00 22.70 ? 406 ASP B O   1 
ATOM   5413 C  CB  . ASP B 1 406 ? -20.376 -8.058  31.732  1.00 23.20 ? 406 ASP B CB  1 
ATOM   5414 C  CG  . ASP B 1 406 ? -21.450 -6.963  31.758  1.00 25.60 ? 406 ASP B CG  1 
ATOM   5415 O  OD1 . ASP B 1 406 ? -21.464 -6.046  30.884  1.00 24.53 ? 406 ASP B OD1 1 
ATOM   5416 O  OD2 . ASP B 1 406 ? -22.208 -6.941  32.698  1.00 32.02 ? 406 ASP B OD2 1 
ATOM   5417 N  N   . ALA B 1 407 ? -19.666 -7.783  28.884  1.00 24.42 ? 407 ALA B N   1 
ATOM   5418 C  CA  . ALA B 1 407 ? -19.619 -7.476  27.465  1.00 22.71 ? 407 ALA B CA  1 
ATOM   5419 C  C   . ALA B 1 407 ? -20.508 -6.302  27.069  1.00 19.81 ? 407 ALA B C   1 
ATOM   5420 O  O   . ALA B 1 407 ? -20.368 -5.752  26.007  1.00 29.23 ? 407 ALA B O   1 
ATOM   5421 C  CB  . ALA B 1 407 ? -19.953 -8.761  26.706  1.00 27.78 ? 407 ALA B CB  1 
ATOM   5422 N  N   . ASP B 1 408 ? -21.363 -5.808  27.946  1.00 23.77 ? 408 ASP B N   1 
ATOM   5423 C  CA  . ASP B 1 408 ? -22.256 -4.707  27.639  1.00 25.54 ? 408 ASP B CA  1 
ATOM   5424 C  C   . ASP B 1 408 ? -21.714 -3.379  28.209  1.00 24.79 ? 408 ASP B C   1 
ATOM   5425 O  O   . ASP B 1 408 ? -22.130 -2.312  27.807  1.00 29.25 ? 408 ASP B O   1 
ATOM   5426 C  CB  . ASP B 1 408 ? -23.657 -4.934  28.201  1.00 31.00 ? 408 ASP B CB  1 
ATOM   5427 C  CG  . ASP B 1 408 ? -24.400 -6.101  27.558  1.00 30.49 ? 408 ASP B CG  1 
ATOM   5428 O  OD1 . ASP B 1 408 ? -24.269 -6.317  26.345  1.00 41.97 ? 408 ASP B OD1 1 
ATOM   5429 O  OD2 . ASP B 1 408 ? -25.127 -6.726  28.281  1.00 38.89 ? 408 ASP B OD2 1 
ATOM   5430 N  N   . ASP B 1 409 ? -20.725 -3.466  29.083  1.00 19.92 ? 409 ASP B N   1 
ATOM   5431 C  CA  . ASP B 1 409 ? -20.131 -2.309  29.739  1.00 19.05 ? 409 ASP B CA  1 
ATOM   5432 C  C   . ASP B 1 409 ? -19.078 -1.667  28.811  1.00 20.69 ? 409 ASP B C   1 
ATOM   5433 O  O   . ASP B 1 409 ? -18.662 -2.238  27.781  1.00 17.11 ? 409 ASP B O   1 
ATOM   5434 C  CB  . ASP B 1 409 ? -19.525 -2.761  31.086  1.00 16.89 ? 409 ASP B CB  1 
ATOM   5435 C  CG  . ASP B 1 409 ? -19.234 -1.613  32.016  1.00 16.94 ? 409 ASP B CG  1 
ATOM   5436 O  OD1 . ASP B 1 409 ? -19.826 -0.540  31.784  1.00 16.66 ? 409 ASP B OD1 1 
ATOM   5437 O  OD2 . ASP B 1 409 ? -18.603 -1.849  33.037  1.00 18.70 ? 409 ASP B OD2 1 
ATOM   5438 N  N   . TRP B 1 410 ? -18.600 -0.477  29.206  1.00 15.71 ? 410 TRP B N   1 
ATOM   5439 C  CA  . TRP B 1 410 ? -17.679 0.248   28.355  1.00 15.49 ? 410 TRP B CA  1 
ATOM   5440 C  C   . TRP B 1 410 ? -16.845 1.175   29.230  1.00 15.31 ? 410 TRP B C   1 
ATOM   5441 O  O   . TRP B 1 410 ? -17.254 1.560   30.336  1.00 15.31 ? 410 TRP B O   1 
ATOM   5442 C  CB  . TRP B 1 410 ? -18.421 1.000   27.229  1.00 16.00 ? 410 TRP B CB  1 
ATOM   5443 C  CG  . TRP B 1 410 ? -19.651 1.720   27.679  1.00 16.68 ? 410 TRP B CG  1 
ATOM   5444 C  CD1 . TRP B 1 410 ? -20.901 1.147   27.808  1.00 20.98 ? 410 TRP B CD1 1 
ATOM   5445 C  CD2 . TRP B 1 410 ? -19.813 3.099   28.034  1.00 16.87 ? 410 TRP B CD2 1 
ATOM   5446 N  NE1 . TRP B 1 410 ? -21.800 2.078   28.229  1.00 19.94 ? 410 TRP B NE1 1 
ATOM   5447 C  CE2 . TRP B 1 410 ? -21.171 3.278   28.391  1.00 17.69 ? 410 TRP B CE2 1 
ATOM   5448 C  CE3 . TRP B 1 410 ? -18.982 4.218   28.039  1.00 17.67 ? 410 TRP B CE3 1 
ATOM   5449 C  CZ2 . TRP B 1 410 ? -21.697 4.528   28.709  1.00 19.46 ? 410 TRP B CZ2 1 
ATOM   5450 C  CZ3 . TRP B 1 410 ? -19.506 5.454   28.333  1.00 19.68 ? 410 TRP B CZ3 1 
ATOM   5451 C  CH2 . TRP B 1 410 ? -20.835 5.599   28.707  1.00 19.07 ? 410 TRP B CH2 1 
ATOM   5452 N  N   . TRP B 1 411 ? -15.641 1.425   28.732  1.00 12.25 ? 411 TRP B N   1 
ATOM   5453 C  CA  . TRP B 1 411 ? -14.691 2.299   29.392  1.00 12.02 ? 411 TRP B CA  1 
ATOM   5454 C  C   . TRP B 1 411 ? -15.337 3.636   29.727  1.00 12.77 ? 411 TRP B C   1 
ATOM   5455 O  O   . TRP B 1 411 ? -15.822 4.286   28.839  1.00 13.70 ? 411 TRP B O   1 
ATOM   5456 C  CB  . TRP B 1 411 ? -13.577 2.522   28.382  1.00 12.31 ? 411 TRP B CB  1 
ATOM   5457 C  CG  . TRP B 1 411 ? -12.504 1.490   28.423  1.00 12.63 ? 411 TRP B CG  1 
ATOM   5458 C  CD1 . TRP B 1 411 ? -12.226 0.603   29.411  1.00 14.09 ? 411 TRP B CD1 1 
ATOM   5459 C  CD2 . TRP B 1 411 ? -11.498 1.338   27.436  1.00 12.47 ? 411 TRP B CD2 1 
ATOM   5460 N  NE1 . TRP B 1 411 ? -11.079 -0.080  29.106  1.00 13.17 ? 411 TRP B NE1 1 
ATOM   5461 C  CE2 . TRP B 1 411 ? -10.607 0.336   27.903  1.00 12.37 ? 411 TRP B CE2 1 
ATOM   5462 C  CE3 . TRP B 1 411 ? -11.215 1.984   26.234  1.00 14.61 ? 411 TRP B CE3 1 
ATOM   5463 C  CZ2 . TRP B 1 411 ? -9.484  -0.062  27.178  1.00 12.54 ? 411 TRP B CZ2 1 
ATOM   5464 C  CZ3 . TRP B 1 411 ? -10.091 1.593   25.528  1.00 13.14 ? 411 TRP B CZ3 1 
ATOM   5465 C  CH2 . TRP B 1 411 ? -9.226  0.616   26.021  1.00 14.62 ? 411 TRP B CH2 1 
ATOM   5466 N  N   . GLY B 1 412 ? -15.274 4.048   30.998  1.00 14.57 ? 412 GLY B N   1 
ATOM   5467 C  CA  . GLY B 1 412 ? -15.810 5.350   31.346  1.00 15.27 ? 412 GLY B CA  1 
ATOM   5468 C  C   . GLY B 1 412 ? -17.301 5.364   31.670  1.00 15.29 ? 412 GLY B C   1 
ATOM   5469 O  O   . GLY B 1 412 ? -17.782 6.433   31.989  1.00 17.16 ? 412 GLY B O   1 
ATOM   5470 N  N   . SER B 1 413 ? -17.972 4.187   31.698  1.00 14.33 ? 413 SER B N   1 
ATOM   5471 C  CA  . SER B 1 413 ? -19.395 4.115   31.891  1.00 14.73 ? 413 SER B CA  1 
ATOM   5472 C  C   . SER B 1 413 ? -19.759 4.691   33.257  1.00 16.99 ? 413 SER B C   1 
ATOM   5473 O  O   . SER B 1 413 ? -20.832 5.261   33.393  1.00 20.52 ? 413 SER B O   1 
ATOM   5474 C  CB  . SER B 1 413 ? -19.950 2.708   31.769  1.00 16.04 ? 413 SER B CB  1 
ATOM   5475 O  OG  . SER B 1 413 ? -19.461 1.915   32.836  1.00 16.51 ? 413 SER B OG  1 
ATOM   5476 N  N   . THR B 1 414 ? -18.888 4.546   34.271  1.00 14.68 ? 414 THR B N   1 
ATOM   5477 C  CA  . THR B 1 414 ? -19.305 5.052   35.574  1.00 15.88 ? 414 THR B CA  1 
ATOM   5478 C  C   . THR B 1 414 ? -19.236 6.581   35.605  1.00 17.81 ? 414 THR B C   1 
ATOM   5479 O  O   . THR B 1 414 ? -19.878 7.197   36.451  1.00 20.82 ? 414 THR B O   1 
ATOM   5480 C  CB  . THR B 1 414 ? -18.518 4.479   36.747  1.00 16.76 ? 414 THR B CB  1 
ATOM   5481 O  OG1 . THR B 1 414 ? -17.161 4.919   36.621  1.00 14.62 ? 414 THR B OG1 1 
ATOM   5482 C  CG2 . THR B 1 414 ? -18.583 2.980   36.858  1.00 18.91 ? 414 THR B CG2 1 
ATOM   5483 N  N   . LEU B 1 415 ? -18.449 7.208   34.750  1.00 16.85 ? 415 LEU B N   1 
ATOM   5484 C  CA  . LEU B 1 415 ? -18.296 8.650   34.756  1.00 18.94 ? 415 LEU B CA  1 
ATOM   5485 C  C   . LEU B 1 415 ? -19.367 9.253   33.858  1.00 21.99 ? 415 LEU B C   1 
ATOM   5486 O  O   . LEU B 1 415 ? -19.969 10.280  34.203  1.00 22.60 ? 415 LEU B O   1 
ATOM   5487 C  CB  . LEU B 1 415 ? -16.882 9.013   34.272  1.00 16.52 ? 415 LEU B CB  1 
ATOM   5488 C  CG  . LEU B 1 415 ? -16.661 10.514  34.039  1.00 16.92 ? 415 LEU B CG  1 
ATOM   5489 C  CD1 . LEU B 1 415 ? -16.881 11.330  35.317  1.00 19.41 ? 415 LEU B CD1 1 
ATOM   5490 C  CD2 . LEU B 1 415 ? -15.300 10.735  33.523  1.00 18.31 ? 415 LEU B CD2 1 
ATOM   5491 N  N   . PHE B 1 416 ? -19.536 8.673   32.673  1.00 19.53 ? 416 PHE B N   1 
ATOM   5492 C  CA  . PHE B 1 416 ? -20.415 9.268   31.702  1.00 21.79 ? 416 PHE B CA  1 
ATOM   5493 C  C   . PHE B 1 416 ? -21.849 8.802   31.859  1.00 28.90 ? 416 PHE B C   1 
ATOM   5494 O  O   . PHE B 1 416 ? -22.736 9.527   31.453  1.00 28.47 ? 416 PHE B O   1 
ATOM   5495 C  CB  . PHE B 1 416 ? -19.892 9.026   30.306  1.00 19.42 ? 416 PHE B CB  1 
ATOM   5496 C  CG  . PHE B 1 416 ? -18.713 9.863   29.959  1.00 20.96 ? 416 PHE B CG  1 
ATOM   5497 C  CD1 . PHE B 1 416 ? -18.902 11.163  29.540  1.00 24.26 ? 416 PHE B CD1 1 
ATOM   5498 C  CD2 . PHE B 1 416 ? -17.439 9.404   30.127  1.00 20.05 ? 416 PHE B CD2 1 
ATOM   5499 C  CE1 . PHE B 1 416 ? -17.814 11.959  29.258  1.00 22.37 ? 416 PHE B CE1 1 
ATOM   5500 C  CE2 . PHE B 1 416 ? -16.353 10.213  29.895  1.00 19.88 ? 416 PHE B CE2 1 
ATOM   5501 C  CZ  . PHE B 1 416 ? -16.548 11.497  29.455  1.00 23.66 ? 416 PHE B CZ  1 
ATOM   5502 N  N   . GLY B 1 417 ? -22.105 7.639   32.445  1.00 31.82 ? 417 GLY B N   1 
ATOM   5503 C  CA  . GLY B 1 417 ? -23.457 7.138   32.629  1.00 38.95 ? 417 GLY B CA  1 
ATOM   5504 C  C   . GLY B 1 417 ? -23.832 6.204   31.496  1.00 36.36 ? 417 GLY B C   1 
ATOM   5505 O  O   . GLY B 1 417 ? -25.058 5.870   31.423  1.00 53.06 ? 417 GLY B O   1 
HETATM 5506 C  CHA . HEM C 2 .   ? 9.557   -7.412  -1.497  1.00 10.92 ? 501 HEM A CHA 1 
HETATM 5507 C  CHB . HEM C 2 .   ? 7.523   -4.139  1.407   1.00 12.04 ? 501 HEM A CHB 1 
HETATM 5508 C  CHC . HEM C 2 .   ? 11.277  -1.215  0.668   1.00 11.82 ? 501 HEM A CHC 1 
HETATM 5509 C  CHD . HEM C 2 .   ? 13.328  -4.614  -2.213  1.00 10.61 ? 501 HEM A CHD 1 
HETATM 5510 C  C1A . HEM C 2 .   ? 8.661   -6.764  -0.657  1.00 11.94 ? 501 HEM A C1A 1 
HETATM 5511 C  C2A . HEM C 2 .   ? 7.428   -7.341  -0.221  1.00 10.01 ? 501 HEM A C2A 1 
HETATM 5512 C  C3A . HEM C 2 .   ? 6.866   -6.425  0.598   1.00 10.96 ? 501 HEM A C3A 1 
HETATM 5513 C  C4A . HEM C 2 .   ? 7.717   -5.305  0.654   1.00 11.66 ? 501 HEM A C4A 1 
HETATM 5514 C  CMA . HEM C 2 .   ? 5.520   -6.531  1.335   1.00 12.21 ? 501 HEM A CMA 1 
HETATM 5515 C  CAA . HEM C 2 .   ? 6.752   -8.676  -0.583  1.00 10.35 ? 501 HEM A CAA 1 
HETATM 5516 C  CBA . HEM C 2 .   ? 7.205   -9.917  0.248   1.00 10.15 ? 501 HEM A CBA 1 
HETATM 5517 C  CGA . HEM C 2 .   ? 8.669   -10.194 0.071   1.00 10.83 ? 501 HEM A CGA 1 
HETATM 5518 O  O1A . HEM C 2 .   ? 9.466   -9.739  0.889   1.00 11.96 ? 501 HEM A O1A 1 
HETATM 5519 O  O2A . HEM C 2 .   ? 9.053   -10.969 -0.858  1.00 11.26 ? 501 HEM A O2A 1 
HETATM 5520 C  C1B . HEM C 2 .   ? 8.426   -3.102  1.502   1.00 9.79  ? 501 HEM A C1B 1 
HETATM 5521 C  C2B . HEM C 2 .   ? 8.189   -1.902  2.275   1.00 10.67 ? 501 HEM A C2B 1 
HETATM 5522 C  C3B . HEM C 2 .   ? 9.228   -1.030  2.043   1.00 12.01 ? 501 HEM A C3B 1 
HETATM 5523 C  C4B . HEM C 2 .   ? 10.095  -1.740  1.122   1.00 13.19 ? 501 HEM A C4B 1 
HETATM 5524 C  CMB . HEM C 2 .   ? 7.027   -1.699  3.141   1.00 9.78  ? 501 HEM A CMB 1 
HETATM 5525 C  CAB . HEM C 2 .   ? 9.600   0.251   2.671   1.00 12.78 ? 501 HEM A CAB 1 
HETATM 5526 C  CBB . HEM C 2 .   ? 9.004   0.803   3.681   1.00 14.79 ? 501 HEM A CBB 1 
HETATM 5527 C  C1C . HEM C 2 .   ? 12.188  -1.838  -0.202  1.00 12.67 ? 501 HEM A C1C 1 
HETATM 5528 C  C2C . HEM C 2 .   ? 13.363  -1.263  -0.709  1.00 13.61 ? 501 HEM A C2C 1 
HETATM 5529 C  C3C . HEM C 2 .   ? 13.929  -2.229  -1.454  1.00 11.82 ? 501 HEM A C3C 1 
HETATM 5530 C  C4C . HEM C 2 .   ? 13.092  -3.388  -1.518  1.00 11.54 ? 501 HEM A C4C 1 
HETATM 5531 C  CMC . HEM C 2 .   ? 13.953  0.080   -0.342  1.00 13.54 ? 501 HEM A CMC 1 
HETATM 5532 C  CAC . HEM C 2 .   ? 15.095  -2.282  -2.255  1.00 16.32 ? 501 HEM A CAC 1 
HETATM 5533 C  CBC . HEM C 2 .   ? 15.707  -1.238  -2.782  1.00 18.46 ? 501 HEM A CBC 1 
HETATM 5534 C  C1D . HEM C 2 .   ? 12.472  -5.674  -2.175  1.00 10.19 ? 501 HEM A C1D 1 
HETATM 5535 C  C2D . HEM C 2 .   ? 12.755  -6.938  -2.901  1.00 11.61 ? 501 HEM A C2D 1 
HETATM 5536 C  C3D . HEM C 2 .   ? 11.671  -7.717  -2.664  1.00 11.64 ? 501 HEM A C3D 1 
HETATM 5537 C  C4D . HEM C 2 .   ? 10.757  -6.886  -1.886  1.00 11.11 ? 501 HEM A C4D 1 
HETATM 5538 C  CMD . HEM C 2 .   ? 14.047  -7.222  -3.641  1.00 15.11 ? 501 HEM A CMD 1 
HETATM 5539 C  CAD . HEM C 2 .   ? 11.478  -9.108  -3.176  1.00 12.23 ? 501 HEM A CAD 1 
HETATM 5540 C  CBD . HEM C 2 .   ? 10.978  -9.131  -4.627  1.00 12.82 ? 501 HEM A CBD 1 
HETATM 5541 C  CGD . HEM C 2 .   ? 10.941  -10.560 -5.138  1.00 12.84 ? 501 HEM A CGD 1 
HETATM 5542 O  O1D . HEM C 2 .   ? 9.859   -11.221 -5.207  1.00 14.40 ? 501 HEM A O1D 1 
HETATM 5543 O  O2D . HEM C 2 .   ? 11.996  -11.115 -5.474  1.00 16.54 ? 501 HEM A O2D 1 
HETATM 5544 N  NA  . HEM C 2 .   ? 8.824   -5.479  -0.111  1.00 12.05 ? 501 HEM A NA  1 
HETATM 5545 N  NB  . HEM C 2 .   ? 9.586   -2.931  0.864   1.00 11.48 ? 501 HEM A NB  1 
HETATM 5546 N  NC  . HEM C 2 .   ? 12.038  -3.095  -0.718  1.00 10.41 ? 501 HEM A NC  1 
HETATM 5547 N  ND  . HEM C 2 .   ? 11.283  -5.698  -1.604  1.00 10.60 ? 501 HEM A ND  1 
HETATM 5548 FE FE  . HEM C 2 .   ? 10.364  -4.267  -0.515  1.00 12.23 ? 501 HEM A FE  1 
HETATM 5549 C  CHA . HEM D 2 .   ? 13.377  1.213   45.214  1.00 12.61 ? 501 HEM B CHA 1 
HETATM 5550 C  CHB . HEM D 2 .   ? 15.758  2.589   41.267  1.00 13.03 ? 501 HEM B CHB 1 
HETATM 5551 C  CHC . HEM D 2 .   ? 12.832  6.494   40.744  1.00 10.76 ? 501 HEM B CHC 1 
HETATM 5552 C  CHD . HEM D 2 .   ? 10.294  4.968   44.497  1.00 11.12 ? 501 HEM B CHD 1 
HETATM 5553 C  C1A . HEM D 2 .   ? 14.307  1.305   44.220  1.00 13.70 ? 501 HEM B C1A 1 
HETATM 5554 C  C2A . HEM D 2 .   ? 15.343  0.372   44.043  1.00 13.12 ? 501 HEM B C2A 1 
HETATM 5555 C  C3A . HEM D 2 .   ? 16.000  0.754   42.914  1.00 14.28 ? 501 HEM B C3A 1 
HETATM 5556 C  C4A . HEM D 2 .   ? 15.373  1.883   42.395  1.00 12.11 ? 501 HEM B C4A 1 
HETATM 5557 C  CMA . HEM D 2 .   ? 17.269  0.093   42.379  1.00 15.30 ? 501 HEM B CMA 1 
HETATM 5558 C  CAA . HEM D 2 .   ? 15.718  -0.770  44.902  1.00 15.80 ? 501 HEM B CAA 1 
HETATM 5559 C  CBA . HEM D 2 .   ? 15.022  -2.098  44.693  1.00 14.78 ? 501 HEM B CBA 1 
HETATM 5560 C  CGA . HEM D 2 .   ? 13.548  -2.081  44.797  1.00 14.82 ? 501 HEM B CGA 1 
HETATM 5561 O  O1A . HEM D 2 .   ? 12.868  -1.827  43.772  1.00 16.54 ? 501 HEM B O1A 1 
HETATM 5562 O  O2A . HEM D 2 .   ? 13.001  -2.279  45.892  1.00 14.89 ? 501 HEM B O2A 1 
HETATM 5563 C  C1B . HEM D 2 .   ? 15.173  3.784   40.744  1.00 12.46 ? 501 HEM B C1B 1 
HETATM 5564 C  C2B . HEM D 2 .   ? 15.575  4.411   39.562  1.00 12.67 ? 501 HEM B C2B 1 
HETATM 5565 C  C3B . HEM D 2 .   ? 14.791  5.498   39.500  1.00 13.93 ? 501 HEM B C3B 1 
HETATM 5566 C  C4B . HEM D 2 .   ? 13.836  5.530   40.576  1.00 11.43 ? 501 HEM B C4B 1 
HETATM 5567 C  CMB . HEM D 2 .   ? 16.783  3.948   38.702  1.00 14.65 ? 501 HEM B CMB 1 
HETATM 5568 C  CAB . HEM D 2 .   ? 14.748  6.541   38.409  1.00 14.24 ? 501 HEM B CAB 1 
HETATM 5569 C  CBB . HEM D 2 .   ? 15.385  6.405   37.263  1.00 15.70 ? 501 HEM B CBB 1 
HETATM 5570 C  C1C . HEM D 2 .   ? 11.864  6.434   41.750  1.00 12.82 ? 501 HEM B C1C 1 
HETATM 5571 C  C2C . HEM D 2 .   ? 10.810  7.327   41.907  1.00 11.58 ? 501 HEM B C2C 1 
HETATM 5572 C  C3C . HEM D 2 .   ? 10.091  6.890   42.985  1.00 12.48 ? 501 HEM B C3C 1 
HETATM 5573 C  C4C . HEM D 2 .   ? 10.752  5.698   43.504  1.00 11.74 ? 501 HEM B C4C 1 
HETATM 5574 C  CMC . HEM D 2 .   ? 10.579  8.491   40.985  1.00 12.38 ? 501 HEM B CMC 1 
HETATM 5575 C  CAC . HEM D 2 .   ? 8.871   7.442   43.617  1.00 11.38 ? 501 HEM B CAC 1 
HETATM 5576 C  CBC . HEM D 2 .   ? 8.577   8.657   43.618  1.00 12.88 ? 501 HEM B CBC 1 
HETATM 5577 C  C1D . HEM D 2 .   ? 10.929  3.757   44.959  1.00 12.40 ? 501 HEM B C1D 1 
HETATM 5578 C  C2D . HEM D 2 .   ? 10.401  2.963   46.093  1.00 11.76 ? 501 HEM B C2D 1 
HETATM 5579 C  C3D . HEM D 2 .   ? 11.300  1.931   46.316  1.00 12.02 ? 501 HEM B C3D 1 
HETATM 5580 C  C4D . HEM D 2 .   ? 12.327  2.112   45.278  1.00 11.29 ? 501 HEM B C4D 1 
HETATM 5581 C  CMD . HEM D 2 .   ? 9.169   3.300   46.781  1.00 14.16 ? 501 HEM B CMD 1 
HETATM 5582 C  CAD . HEM D 2 .   ? 11.190  0.800   47.341  1.00 13.91 ? 501 HEM B CAD 1 
HETATM 5583 C  CBD . HEM D 2 .   ? 11.712  1.366   48.640  1.00 16.20 ? 501 HEM B CBD 1 
HETATM 5584 C  CGD . HEM D 2 .   ? 11.540  0.235   49.704  1.00 13.70 ? 501 HEM B CGD 1 
HETATM 5585 O  O1D . HEM D 2 .   ? 12.456  -0.569  49.985  1.00 16.94 ? 501 HEM B O1D 1 
HETATM 5586 O  O2D . HEM D 2 .   ? 10.394  0.061   50.152  1.00 16.76 ? 501 HEM B O2D 1 
HETATM 5587 N  NA  . HEM D 2 .   ? 14.315  2.237   43.166  1.00 12.68 ? 501 HEM B NA  1 
HETATM 5588 N  NB  . HEM D 2 .   ? 14.085  4.377   41.240  1.00 12.74 ? 501 HEM B NB  1 
HETATM 5589 N  NC  . HEM D 2 .   ? 11.843  5.414   42.687  1.00 12.09 ? 501 HEM B NC  1 
HETATM 5590 N  ND  . HEM D 2 .   ? 12.087  3.232   44.518  1.00 12.88 ? 501 HEM B ND  1 
HETATM 5591 FE FE  . HEM D 2 .   ? 13.215  3.962   43.070  1.00 12.59 ? 501 HEM B FE  1 
HETATM 5592 O  O   . HOH E 3 .   ? 1.182   -20.329 2.946   1.00 33.48 ? 601 HOH A O   1 
HETATM 5593 O  O   . HOH E 3 .   ? 17.242  -2.729  -12.666 1.00 30.42 ? 602 HOH A O   1 
HETATM 5594 O  O   . HOH E 3 .   ? 10.690  2.047   -12.369 1.00 31.77 ? 603 HOH A O   1 
HETATM 5595 O  O   . HOH E 3 .   ? -7.295  -9.659  0.896   1.00 35.86 ? 604 HOH A O   1 
HETATM 5596 O  O   . HOH E 3 .   ? 7.477   -5.060  12.099  1.00 28.41 ? 605 HOH A O   1 
HETATM 5597 O  O   . HOH E 3 .   ? 39.042  -7.438  8.261   1.00 31.09 ? 606 HOH A O   1 
HETATM 5598 O  O   . HOH E 3 .   ? 23.688  -9.052  -4.865  1.00 23.69 ? 607 HOH A O   1 
HETATM 5599 O  O   . HOH E 3 .   ? 16.792  -15.870 22.505  1.00 25.98 ? 608 HOH A O   1 
HETATM 5600 O  O   . HOH E 3 .   ? 34.592  -6.445  -2.863  1.00 20.09 ? 609 HOH A O   1 
HETATM 5601 O  O   . HOH E 3 .   ? 4.801   -17.094 6.680   1.00 21.67 ? 610 HOH A O   1 
HETATM 5602 O  O   . HOH E 3 .   ? -1.615  -21.312 -6.171  1.00 33.09 ? 611 HOH A O   1 
HETATM 5603 O  O   . HOH E 3 .   ? -6.592  10.982  6.694   1.00 22.86 ? 612 HOH A O   1 
HETATM 5604 O  O   . HOH E 3 .   ? 7.184   -19.348 12.572  1.00 37.06 ? 613 HOH A O   1 
HETATM 5605 O  O   . HOH E 3 .   ? 31.382  -14.692 -3.327  1.00 25.44 ? 614 HOH A O   1 
HETATM 5606 O  O   . HOH E 3 .   ? -3.517  5.809   11.080  1.00 17.65 ? 615 HOH A O   1 
HETATM 5607 O  O   . HOH E 3 .   ? 7.882   -8.077  13.502  1.00 29.36 ? 616 HOH A O   1 
HETATM 5608 O  O   . HOH E 3 .   ? 37.791  -15.062 -5.944  1.00 45.37 ? 617 HOH A O   1 
HETATM 5609 O  O   . HOH E 3 .   ? 31.242  -9.904  14.013  1.00 14.41 ? 618 HOH A O   1 
HETATM 5610 O  O   . HOH E 3 .   ? 7.958   -10.963 -3.242  1.00 13.99 ? 619 HOH A O   1 
HETATM 5611 O  O   . HOH E 3 .   ? 37.028  -11.937 25.316  1.00 20.56 ? 620 HOH A O   1 
HETATM 5612 O  O   . HOH E 3 .   ? 8.048   -21.324 -4.776  1.00 32.72 ? 621 HOH A O   1 
HETATM 5613 O  O   . HOH E 3 .   ? 5.291   8.020   10.127  1.00 25.69 ? 622 HOH A O   1 
HETATM 5614 O  O   . HOH E 3 .   ? 28.494  -16.806 20.961  1.00 28.26 ? 623 HOH A O   1 
HETATM 5615 O  O   . HOH E 3 .   ? 10.041  -15.811 -8.892  1.00 22.54 ? 624 HOH A O   1 
HETATM 5616 O  O   . HOH E 3 .   ? 36.840  -8.275  -2.943  1.00 26.05 ? 625 HOH A O   1 
HETATM 5617 O  O   . HOH E 3 .   ? 36.929  -8.715  10.650  1.00 27.34 ? 626 HOH A O   1 
HETATM 5618 O  O   . HOH E 3 .   ? 0.668   4.729   -5.364  1.00 25.63 ? 627 HOH A O   1 
HETATM 5619 O  O   . HOH E 3 .   ? -5.244  -4.651  6.871   1.00 16.50 ? 628 HOH A O   1 
HETATM 5620 O  O   . HOH E 3 .   ? 34.865  -1.829  29.829  1.00 31.70 ? 629 HOH A O   1 
HETATM 5621 O  O   . HOH E 3 .   ? 0.236   -0.538  -8.220  1.00 25.04 ? 630 HOH A O   1 
HETATM 5622 O  O   . HOH E 3 .   ? 37.244  -15.694 -3.285  1.00 40.13 ? 631 HOH A O   1 
HETATM 5623 O  O   . HOH E 3 .   ? 47.918  -0.837  18.332  1.00 29.71 ? 632 HOH A O   1 
HETATM 5624 O  O   . HOH E 3 .   ? 24.342  6.929   1.873   1.00 29.27 ? 633 HOH A O   1 
HETATM 5625 O  O   . HOH E 3 .   ? 19.687  -7.878  33.697  1.00 22.41 ? 634 HOH A O   1 
HETATM 5626 O  O   . HOH E 3 .   ? -8.262  -6.616  -2.850  1.00 36.09 ? 635 HOH A O   1 
HETATM 5627 O  O   . HOH E 3 .   ? 31.007  7.294   5.605   1.00 39.17 ? 636 HOH A O   1 
HETATM 5628 O  O   . HOH E 3 .   ? 5.628   5.639   19.142  1.00 27.49 ? 637 HOH A O   1 
HETATM 5629 O  O   . HOH E 3 .   ? 25.150  -17.244 12.293  1.00 26.77 ? 638 HOH A O   1 
HETATM 5630 O  O   . HOH E 3 .   ? 10.019  -8.270  -15.171 1.00 36.63 ? 639 HOH A O   1 
HETATM 5631 O  O   . HOH E 3 .   ? 11.010  -3.773  3.713   1.00 14.92 ? 640 HOH A O   1 
HETATM 5632 O  O   . HOH E 3 .   ? 32.622  -7.573  -4.249  1.00 23.30 ? 641 HOH A O   1 
HETATM 5633 O  O   . HOH E 3 .   ? 14.796  -15.272 9.934   1.00 15.82 ? 642 HOH A O   1 
HETATM 5634 O  O   . HOH E 3 .   ? -3.314  14.871  12.538  1.00 15.30 ? 643 HOH A O   1 
HETATM 5635 O  O   . HOH E 3 .   ? 33.045  -13.855 12.571  1.00 19.00 ? 644 HOH A O   1 
HETATM 5636 O  O   . HOH E 3 .   ? 28.106  -2.913  36.861  1.00 20.37 ? 645 HOH A O   1 
HETATM 5637 O  O   . HOH E 3 .   ? 12.281  -7.870  4.332   1.00 14.12 ? 646 HOH A O   1 
HETATM 5638 O  O   . HOH E 3 .   ? 4.392   -12.442 1.212   1.00 15.67 ? 647 HOH A O   1 
HETATM 5639 O  O   . HOH E 3 .   ? -5.585  -23.742 1.145   1.00 32.89 ? 648 HOH A O   1 
HETATM 5640 O  O   . HOH E 3 .   ? 11.709  -16.110 3.800   1.00 22.73 ? 649 HOH A O   1 
HETATM 5641 O  O   . HOH E 3 .   ? 7.645   -1.313  9.310   1.00 15.05 ? 650 HOH A O   1 
HETATM 5642 O  O   . HOH E 3 .   ? 9.807   2.270   -3.198  1.00 19.85 ? 651 HOH A O   1 
HETATM 5643 O  O   . HOH E 3 .   ? 34.662  -4.572  37.075  1.00 29.11 ? 652 HOH A O   1 
HETATM 5644 O  O   . HOH E 3 .   ? 39.363  -12.698 8.774   1.00 39.83 ? 653 HOH A O   1 
HETATM 5645 O  O   . HOH E 3 .   ? 12.301  2.644   -2.029  1.00 22.23 ? 654 HOH A O   1 
HETATM 5646 O  O   . HOH E 3 .   ? 26.129  -14.144 8.840   1.00 14.75 ? 655 HOH A O   1 
HETATM 5647 O  O   . HOH E 3 .   ? 34.885  -1.942  40.416  1.00 24.72 ? 656 HOH A O   1 
HETATM 5648 O  O   . HOH E 3 .   ? 24.462  -8.267  14.176  1.00 13.10 ? 657 HOH A O   1 
HETATM 5649 O  O   . HOH E 3 .   ? 25.100  -7.520  25.802  1.00 17.69 ? 658 HOH A O   1 
HETATM 5650 O  O   . HOH E 3 .   ? 28.580  7.399   1.198   1.00 37.87 ? 659 HOH A O   1 
HETATM 5651 O  O   . HOH E 3 .   ? 14.252  -11.624 -4.008  1.00 15.77 ? 660 HOH A O   1 
HETATM 5652 O  O   . HOH E 3 .   ? -10.239 0.577   -4.563  1.00 32.25 ? 661 HOH A O   1 
HETATM 5653 O  O   . HOH E 3 .   ? 15.613  -9.869  -1.224  1.00 15.75 ? 662 HOH A O   1 
HETATM 5654 O  O   . HOH E 3 .   ? 24.880  -15.033 20.887  1.00 12.90 ? 663 HOH A O   1 
HETATM 5655 O  O   . HOH E 3 .   ? 20.548  8.464   -1.865  1.00 23.58 ? 664 HOH A O   1 
HETATM 5656 O  O   . HOH E 3 .   ? 10.928  -15.846 9.618   1.00 21.92 ? 665 HOH A O   1 
HETATM 5657 O  O   . HOH E 3 .   ? 19.946  -10.232 37.056  1.00 30.32 ? 666 HOH A O   1 
HETATM 5658 O  O   . HOH E 3 .   ? 17.772  -0.241  -12.566 1.00 26.37 ? 667 HOH A O   1 
HETATM 5659 O  O   . HOH E 3 .   ? 36.720  9.776   9.152   1.00 39.43 ? 668 HOH A O   1 
HETATM 5660 O  O   . HOH E 3 .   ? 6.673   -16.105 -3.449  1.00 19.30 ? 669 HOH A O   1 
HETATM 5661 O  O   . HOH E 3 .   ? 16.007  -7.935  -6.190  1.00 16.49 ? 670 HOH A O   1 
HETATM 5662 O  O   . HOH E 3 .   ? 9.833   -16.503 6.490   1.00 17.83 ? 671 HOH A O   1 
HETATM 5663 O  O   . HOH E 3 .   ? 25.942  -7.027  32.391  1.00 17.53 ? 672 HOH A O   1 
HETATM 5664 O  O   . HOH E 3 .   ? 34.673  9.726   22.402  1.00 37.05 ? 673 HOH A O   1 
HETATM 5665 O  O   . HOH E 3 .   ? 27.329  -13.975 17.818  1.00 16.18 ? 674 HOH A O   1 
HETATM 5666 O  O   . HOH E 3 .   ? 15.342  -9.934  30.110  1.00 20.30 ? 675 HOH A O   1 
HETATM 5667 O  O   . HOH E 3 .   ? 32.502  -20.671 15.034  1.00 33.36 ? 676 HOH A O   1 
HETATM 5668 O  O   . HOH E 3 .   ? -3.598  9.959   15.192  1.00 21.67 ? 677 HOH A O   1 
HETATM 5669 O  O   . HOH E 3 .   ? 19.242  -18.287 8.393   1.00 20.55 ? 678 HOH A O   1 
HETATM 5670 O  O   . HOH E 3 .   ? -5.961  7.723   7.903   1.00 21.87 ? 679 HOH A O   1 
HETATM 5671 O  O   . HOH E 3 .   ? 14.882  14.422  6.682   1.00 32.23 ? 680 HOH A O   1 
HETATM 5672 O  O   . HOH E 3 .   ? 18.076  14.347  0.521   1.00 24.84 ? 681 HOH A O   1 
HETATM 5673 O  O   . HOH E 3 .   ? 14.982  -16.095 13.724  1.00 23.57 ? 682 HOH A O   1 
HETATM 5674 O  O   . HOH E 3 .   ? 32.227  -0.942  29.379  1.00 31.03 ? 683 HOH A O   1 
HETATM 5675 O  O   . HOH E 3 .   ? 27.658  -17.783 13.421  1.00 35.11 ? 684 HOH A O   1 
HETATM 5676 O  O   . HOH E 3 .   ? 36.904  7.651   1.158   1.00 33.81 ? 685 HOH A O   1 
HETATM 5677 O  O   . HOH E 3 .   ? 43.971  -11.086 9.208   1.00 36.32 ? 686 HOH A O   1 
HETATM 5678 O  O   . HOH E 3 .   ? 25.445  -10.060 26.476  1.00 13.86 ? 687 HOH A O   1 
HETATM 5679 O  O   . HOH E 3 .   ? 31.624  -11.106 6.848   1.00 14.88 ? 688 HOH A O   1 
HETATM 5680 O  O   . HOH E 3 .   ? 32.053  6.233   22.186  1.00 26.35 ? 689 HOH A O   1 
HETATM 5681 O  O   . HOH E 3 .   ? 14.719  5.575   -7.565  1.00 22.34 ? 690 HOH A O   1 
HETATM 5682 O  O   . HOH E 3 .   ? 9.781   -2.487  23.102  1.00 34.93 ? 691 HOH A O   1 
HETATM 5683 O  O   . HOH E 3 .   ? 19.867  -7.003  10.440  1.00 15.65 ? 692 HOH A O   1 
HETATM 5684 O  O   . HOH E 3 .   ? 15.831  4.615   17.591  1.00 24.20 ? 693 HOH A O   1 
HETATM 5685 O  O   . HOH E 3 .   ? 32.699  -18.151 26.678  1.00 28.78 ? 694 HOH A O   1 
HETATM 5686 O  O   . HOH E 3 .   ? 1.328   -13.394 -9.721  1.00 19.30 ? 695 HOH A O   1 
HETATM 5687 O  O   . HOH E 3 .   ? -4.445  7.174   0.405   1.00 25.48 ? 696 HOH A O   1 
HETATM 5688 O  O   . HOH E 3 .   ? 12.456  -13.746 10.416  1.00 17.21 ? 697 HOH A O   1 
HETATM 5689 O  O   . HOH E 3 .   ? 23.417  -11.692 27.764  1.00 20.44 ? 698 HOH A O   1 
HETATM 5690 O  O   . HOH E 3 .   ? 17.771  -14.570 -7.396  1.00 25.30 ? 699 HOH A O   1 
HETATM 5691 O  O   . HOH E 3 .   ? 11.188  -5.197  1.542   1.00 12.30 ? 700 HOH A O   1 
HETATM 5692 O  O   . HOH E 3 .   ? 12.064  8.836   -0.660  1.00 20.62 ? 701 HOH A O   1 
HETATM 5693 O  O   . HOH E 3 .   ? 29.267  -16.576 10.739  1.00 23.53 ? 702 HOH A O   1 
HETATM 5694 O  O   . HOH E 3 .   ? 37.676  -10.893 30.497  1.00 35.78 ? 703 HOH A O   1 
HETATM 5695 O  O   . HOH E 3 .   ? -2.703  1.116   -5.620  1.00 41.62 ? 704 HOH A O   1 
HETATM 5696 O  O   . HOH E 3 .   ? 8.760   8.718   -1.922  1.00 30.93 ? 705 HOH A O   1 
HETATM 5697 O  O   . HOH E 3 .   ? 28.701  5.411   6.120   1.00 21.32 ? 706 HOH A O   1 
HETATM 5698 O  O   . HOH E 3 .   ? 30.277  -9.835  36.496  1.00 25.35 ? 707 HOH A O   1 
HETATM 5699 O  O   . HOH E 3 .   ? 37.490  -5.704  26.024  1.00 24.47 ? 708 HOH A O   1 
HETATM 5700 O  O   . HOH E 3 .   ? 3.484   -9.725  1.349   1.00 14.51 ? 709 HOH A O   1 
HETATM 5701 O  O   . HOH E 3 .   ? 25.711  -7.634  -5.530  1.00 26.47 ? 710 HOH A O   1 
HETATM 5702 O  O   . HOH E 3 .   ? 15.831  -2.923  20.154  1.00 26.19 ? 711 HOH A O   1 
HETATM 5703 O  O   . HOH E 3 .   ? 4.745   -10.200 12.264  1.00 22.91 ? 712 HOH A O   1 
HETATM 5704 O  O   . HOH E 3 .   ? -3.051  -6.809  -10.544 1.00 33.57 ? 713 HOH A O   1 
HETATM 5705 O  O   . HOH E 3 .   ? 31.443  -15.689 21.726  1.00 31.89 ? 714 HOH A O   1 
HETATM 5706 O  O   . HOH E 3 .   ? 15.454  -4.553  4.950   1.00 19.53 ? 715 HOH A O   1 
HETATM 5707 O  O   . HOH E 3 .   ? 30.283  -12.527 14.278  1.00 14.78 ? 716 HOH A O   1 
HETATM 5708 O  O   . HOH E 3 .   ? 30.397  -19.888 27.934  1.00 25.96 ? 717 HOH A O   1 
HETATM 5709 O  O   . HOH E 3 .   ? 43.956  -3.658  22.618  1.00 39.85 ? 718 HOH A O   1 
HETATM 5710 O  O   . HOH E 3 .   ? 35.455  -4.128  -4.416  1.00 25.94 ? 719 HOH A O   1 
HETATM 5711 O  O   . HOH E 3 .   ? 1.130   -9.974  3.313   1.00 16.01 ? 720 HOH A O   1 
HETATM 5712 O  O   . HOH E 3 .   ? 11.904  5.490   -3.684  1.00 35.39 ? 721 HOH A O   1 
HETATM 5713 O  O   . HOH E 3 .   ? -2.689  -6.368  -8.050  1.00 24.37 ? 722 HOH A O   1 
HETATM 5714 O  O   . HOH E 3 .   ? 36.025  -7.993  27.524  1.00 21.91 ? 723 HOH A O   1 
HETATM 5715 O  O   . HOH E 3 .   ? 20.246  17.350  6.451   1.00 34.56 ? 724 HOH A O   1 
HETATM 5716 O  O   . HOH E 3 .   ? 7.320   -18.803 5.554   1.00 26.43 ? 725 HOH A O   1 
HETATM 5717 O  O   . HOH E 3 .   ? 27.014  -9.490  28.743  1.00 18.74 ? 726 HOH A O   1 
HETATM 5718 O  O   . HOH E 3 .   ? -4.108  -0.003  6.766   1.00 21.70 ? 727 HOH A O   1 
HETATM 5719 O  O   . HOH E 3 .   ? -0.219  -5.200  -8.484  1.00 18.12 ? 728 HOH A O   1 
HETATM 5720 O  O   . HOH E 3 .   ? 28.319  -11.794 16.332  1.00 13.49 ? 729 HOH A O   1 
HETATM 5721 O  O   . HOH E 3 .   ? 5.490   -17.461 -12.600 1.00 28.97 ? 730 HOH A O   1 
HETATM 5722 O  O   . HOH E 3 .   ? 8.577   -18.193 -2.929  1.00 27.12 ? 731 HOH A O   1 
HETATM 5723 O  O   . HOH E 3 .   ? 5.135   -12.750 -16.094 1.00 29.62 ? 732 HOH A O   1 
HETATM 5724 O  O   . HOH E 3 .   ? 26.212  7.161   -0.030  1.00 25.95 ? 733 HOH A O   1 
HETATM 5725 O  O   . HOH E 3 .   ? 13.986  8.080   -2.416  1.00 33.32 ? 734 HOH A O   1 
HETATM 5726 O  O   . HOH E 3 .   ? 13.546  -16.426 1.138   1.00 28.88 ? 735 HOH A O   1 
HETATM 5727 O  O   . HOH E 3 .   ? 36.246  0.360   34.421  1.00 37.43 ? 736 HOH A O   1 
HETATM 5728 O  O   . HOH E 3 .   ? 33.384  -4.315  39.943  1.00 23.75 ? 737 HOH A O   1 
HETATM 5729 O  O   . HOH E 3 .   ? 32.772  -18.907 17.730  1.00 29.58 ? 738 HOH A O   1 
HETATM 5730 O  O   . HOH E 3 .   ? 23.020  -8.915  -7.641  1.00 27.98 ? 739 HOH A O   1 
HETATM 5731 O  O   . HOH E 3 .   ? 14.853  -14.975 -7.690  1.00 27.38 ? 740 HOH A O   1 
HETATM 5732 O  O   . HOH E 3 .   ? 30.149  -12.846 33.206  1.00 31.48 ? 741 HOH A O   1 
HETATM 5733 O  O   . HOH E 3 .   ? 6.818   -13.967 -13.698 1.00 28.86 ? 742 HOH A O   1 
HETATM 5734 O  O   . HOH E 3 .   ? 30.557  1.189   34.653  1.00 31.02 ? 743 HOH A O   1 
HETATM 5735 O  O   . HOH E 3 .   ? 0.683   -13.512 9.528   1.00 35.45 ? 744 HOH A O   1 
HETATM 5736 O  O   . HOH E 3 .   ? -1.513  7.860   14.480  1.00 19.91 ? 745 HOH A O   1 
HETATM 5737 O  O   . HOH E 3 .   ? 13.885  -10.298 4.391   1.00 15.15 ? 746 HOH A O   1 
HETATM 5738 O  O   . HOH E 3 .   ? -3.204  -13.473 -3.947  1.00 25.29 ? 747 HOH A O   1 
HETATM 5739 O  O   . HOH E 3 .   ? 16.264  -9.673  -4.004  1.00 14.71 ? 748 HOH A O   1 
HETATM 5740 O  O   . HOH E 3 .   ? 20.435  9.173   16.452  1.00 26.34 ? 749 HOH A O   1 
HETATM 5741 O  O   . HOH E 3 .   ? -2.258  -7.900  -5.509  1.00 22.72 ? 750 HOH A O   1 
HETATM 5742 O  O   . HOH E 3 .   ? 10.345  -9.124  16.025  1.00 24.86 ? 751 HOH A O   1 
HETATM 5743 O  O   . HOH E 3 .   ? 39.260  -12.333 23.563  1.00 19.66 ? 752 HOH A O   1 
HETATM 5744 O  O   . HOH E 3 .   ? 28.272  4.400   26.696  1.00 18.44 ? 753 HOH A O   1 
HETATM 5745 O  O   . HOH E 3 .   ? 3.387   -20.803 1.352   1.00 20.06 ? 754 HOH A O   1 
HETATM 5746 O  O   . HOH E 3 .   ? 27.374  6.468   3.831   1.00 27.11 ? 755 HOH A O   1 
HETATM 5747 O  O   . HOH E 3 .   ? -4.125  -15.698 -1.519  1.00 27.10 ? 756 HOH A O   1 
HETATM 5748 O  O   . HOH E 3 .   ? 1.320   9.530   8.894   1.00 24.03 ? 757 HOH A O   1 
HETATM 5749 O  O   . HOH E 3 .   ? 40.805  -14.331 22.886  1.00 28.54 ? 758 HOH A O   1 
HETATM 5750 O  O   . HOH E 3 .   ? 30.933  -17.993 8.926   1.00 28.70 ? 759 HOH A O   1 
HETATM 5751 O  O   . HOH E 3 .   ? 27.801  -19.380 -6.262  1.00 36.15 ? 760 HOH A O   1 
HETATM 5752 O  O   . HOH E 3 .   ? 5.266   -19.811 3.955   1.00 36.44 ? 761 HOH A O   1 
HETATM 5753 O  O   . HOH E 3 .   ? 18.126  -19.926 15.643  1.00 35.32 ? 762 HOH A O   1 
HETATM 5754 O  O   . HOH E 3 .   ? 14.375  -16.410 3.606   1.00 30.92 ? 763 HOH A O   1 
HETATM 5755 O  O   . HOH E 3 .   ? 13.031  -5.229  5.014   1.00 27.33 ? 764 HOH A O   1 
HETATM 5756 O  O   . HOH E 3 .   ? 11.596  1.436   17.413  1.00 21.84 ? 765 HOH A O   1 
HETATM 5757 O  O   . HOH E 3 .   ? 13.198  6.313   -5.971  1.00 45.99 ? 766 HOH A O   1 
HETATM 5758 O  O   . HOH E 3 .   ? -4.295  -9.252  -4.695  1.00 30.32 ? 767 HOH A O   1 
HETATM 5759 O  O   . HOH E 3 .   ? 15.814  -7.550  31.455  1.00 34.36 ? 768 HOH A O   1 
HETATM 5760 O  O   . HOH E 3 .   ? 33.242  -15.379 0.745   1.00 41.45 ? 769 HOH A O   1 
HETATM 5761 O  O   . HOH E 3 .   ? 26.251  -9.566  31.497  1.00 23.65 ? 770 HOH A O   1 
HETATM 5762 O  O   . HOH E 3 .   ? -1.750  8.294   11.370  1.00 27.95 ? 771 HOH A O   1 
HETATM 5763 O  O   . HOH E 3 .   ? 3.566   11.110  6.960   1.00 38.03 ? 772 HOH A O   1 
HETATM 5764 O  O   . HOH E 3 .   ? 16.111  6.670   -9.630  1.00 34.69 ? 773 HOH A O   1 
HETATM 5765 O  O   . HOH E 3 .   ? 37.724  -10.240 27.653  1.00 26.98 ? 774 HOH A O   1 
HETATM 5766 O  O   . HOH E 3 .   ? 26.778  -16.765 9.183   1.00 30.97 ? 775 HOH A O   1 
HETATM 5767 O  O   . HOH E 3 .   ? -3.819  9.756   11.541  1.00 42.65 ? 776 HOH A O   1 
HETATM 5768 O  O   . HOH E 3 .   ? -5.645  7.449   10.572  1.00 22.48 ? 777 HOH A O   1 
HETATM 5769 O  O   . HOH F 3 .   ? -15.892 6.856   17.386  1.00 40.17 ? 601 HOH B O   1 
HETATM 5770 O  O   . HOH F 3 .   ? 12.295  -7.739  51.047  1.00 34.60 ? 602 HOH B O   1 
HETATM 5771 O  O   . HOH F 3 .   ? -21.026 12.625  33.540  1.00 36.64 ? 603 HOH B O   1 
HETATM 5772 O  O   . HOH F 3 .   ? 24.076  13.822  51.613  1.00 32.50 ? 604 HOH B O   1 
HETATM 5773 O  O   . HOH F 3 .   ? -19.761 22.670  21.308  1.00 29.67 ? 605 HOH B O   1 
HETATM 5774 O  O   . HOH F 3 .   ? -17.912 25.845  20.828  1.00 23.08 ? 606 HOH B O   1 
HETATM 5775 O  O   . HOH F 3 .   ? -9.176  -8.895  34.061  1.00 34.63 ? 607 HOH B O   1 
HETATM 5776 O  O   . HOH F 3 .   ? 17.435  -12.641 27.644  1.00 25.96 ? 608 HOH B O   1 
HETATM 5777 O  O   . HOH F 3 .   ? 2.418   16.234  35.738  1.00 27.12 ? 609 HOH B O   1 
HETATM 5778 O  O   . HOH F 3 .   ? 1.328   -5.613  38.453  1.00 34.49 ? 610 HOH B O   1 
HETATM 5779 O  O   . HOH F 3 .   ? 9.198   -10.563 25.179  1.00 27.84 ? 611 HOH B O   1 
HETATM 5780 O  O   . HOH F 3 .   ? -5.296  -5.026  37.182  1.00 12.64 ? 612 HOH B O   1 
HETATM 5781 O  O   . HOH F 3 .   ? -6.930  17.658  44.775  1.00 30.12 ? 613 HOH B O   1 
HETATM 5782 O  O   . HOH F 3 .   ? 13.606  14.136  53.712  1.00 24.82 ? 614 HOH B O   1 
HETATM 5783 O  O   . HOH F 3 .   ? -8.823  -6.301  51.648  1.00 33.60 ? 615 HOH B O   1 
HETATM 5784 O  O   . HOH F 3 .   ? -8.532  9.473   48.478  1.00 28.26 ? 616 HOH B O   1 
HETATM 5785 O  O   . HOH F 3 .   ? -4.753  -9.543  42.145  1.00 29.58 ? 617 HOH B O   1 
HETATM 5786 O  O   . HOH F 3 .   ? -11.414 0.169   12.526  1.00 33.26 ? 618 HOH B O   1 
HETATM 5787 O  O   . HOH F 3 .   ? 6.418   18.034  38.615  1.00 18.82 ? 619 HOH B O   1 
HETATM 5788 O  O   . HOH F 3 .   ? 10.362  -0.913  39.744  1.00 26.87 ? 620 HOH B O   1 
HETATM 5789 O  O   . HOH F 3 .   ? 16.019  -11.754 41.644  1.00 27.97 ? 621 HOH B O   1 
HETATM 5790 O  O   . HOH F 3 .   ? 7.707   -9.484  32.081  1.00 30.93 ? 622 HOH B O   1 
HETATM 5791 O  O   . HOH F 3 .   ? 14.199  -7.365  27.975  1.00 25.19 ? 623 HOH B O   1 
HETATM 5792 O  O   . HOH F 3 .   ? -1.141  -8.415  32.886  1.00 16.95 ? 624 HOH B O   1 
HETATM 5793 O  O   . HOH F 3 .   ? -0.975  -10.649 39.608  1.00 28.93 ? 625 HOH B O   1 
HETATM 5794 O  O   . HOH F 3 .   ? -4.248  -7.948  55.876  1.00 30.33 ? 626 HOH B O   1 
HETATM 5795 O  O   . HOH F 3 .   ? -6.302  22.098  38.695  1.00 37.05 ? 627 HOH B O   1 
HETATM 5796 O  O   . HOH F 3 .   ? 11.435  -3.179  55.365  1.00 30.91 ? 628 HOH B O   1 
HETATM 5797 O  O   . HOH F 3 .   ? 17.343  10.075  55.581  1.00 29.75 ? 629 HOH B O   1 
HETATM 5798 O  O   . HOH F 3 .   ? -13.416 7.260   45.305  1.00 22.96 ? 630 HOH B O   1 
HETATM 5799 O  O   . HOH F 3 .   ? -7.553  18.849  24.295  1.00 28.37 ? 631 HOH B O   1 
HETATM 5800 O  O   . HOH F 3 .   ? 8.402   22.237  27.183  1.00 34.17 ? 632 HOH B O   1 
HETATM 5801 O  O   . HOH F 3 .   ? 28.679  4.942   29.243  1.00 23.72 ? 633 HOH B O   1 
HETATM 5802 O  O   . HOH F 3 .   ? 11.964  2.348   41.325  1.00 25.54 ? 634 HOH B O   1 
HETATM 5803 O  O   . HOH F 3 .   ? -11.022 8.520   44.789  1.00 15.08 ? 635 HOH B O   1 
HETATM 5804 O  O   . HOH F 3 .   ? 14.193  -1.471  48.195  1.00 14.73 ? 636 HOH B O   1 
HETATM 5805 O  O   . HOH F 3 .   ? 4.221   -0.605  53.216  1.00 30.26 ? 637 HOH B O   1 
HETATM 5806 O  O   . HOH F 3 .   ? 15.043  14.582  51.300  1.00 22.30 ? 638 HOH B O   1 
HETATM 5807 O  O   . HOH F 3 .   ? 8.041   8.247   58.500  1.00 33.25 ? 639 HOH B O   1 
HETATM 5808 O  O   . HOH F 3 .   ? -9.703  0.558   48.617  1.00 24.27 ? 640 HOH B O   1 
HETATM 5809 O  O   . HOH F 3 .   ? -0.621  4.450   48.044  1.00 21.11 ? 641 HOH B O   1 
HETATM 5810 O  O   . HOH F 3 .   ? -4.112  18.151  27.009  1.00 28.01 ? 642 HOH B O   1 
HETATM 5811 O  O   . HOH F 3 .   ? -9.159  7.426   46.449  1.00 17.78 ? 643 HOH B O   1 
HETATM 5812 O  O   . HOH F 3 .   ? -11.760 -3.913  2.989   1.00 24.10 ? 644 HOH B O   1 
HETATM 5813 O  O   . HOH F 3 .   ? 5.121   -11.577 34.095  1.00 29.21 ? 645 HOH B O   1 
HETATM 5814 O  O   . HOH F 3 .   ? -2.314  -2.276  30.218  1.00 10.97 ? 646 HOH B O   1 
HETATM 5815 O  O   . HOH F 3 .   ? -13.566 14.001  44.980  1.00 31.46 ? 647 HOH B O   1 
HETATM 5816 O  O   . HOH F 3 .   ? 7.440   11.928  53.187  1.00 32.13 ? 648 HOH B O   1 
HETATM 5817 O  O   . HOH F 3 .   ? 22.772  9.499   28.682  1.00 20.17 ? 649 HOH B O   1 
HETATM 5818 O  O   . HOH F 3 .   ? -9.211  -1.906  30.563  1.00 12.47 ? 650 HOH B O   1 
HETATM 5819 O  O   . HOH F 3 .   ? -8.503  -14.439 15.398  1.00 47.44 ? 651 HOH B O   1 
HETATM 5820 O  O   . HOH F 3 .   ? -8.983  17.439  41.855  1.00 29.67 ? 652 HOH B O   1 
HETATM 5821 O  O   . HOH F 3 .   ? -11.788 -4.568  33.274  1.00 20.78 ? 653 HOH B O   1 
HETATM 5822 O  O   . HOH F 3 .   ? 21.198  16.288  52.100  1.00 20.43 ? 654 HOH B O   1 
HETATM 5823 O  O   . HOH F 3 .   ? 7.290   3.962   49.386  1.00 17.01 ? 655 HOH B O   1 
HETATM 5824 O  O   . HOH F 3 .   ? -8.177  -11.363 26.761  1.00 23.40 ? 656 HOH B O   1 
HETATM 5825 O  O   . HOH F 3 .   ? -3.053  -13.973 46.225  1.00 23.74 ? 657 HOH B O   1 
HETATM 5826 O  O   . HOH F 3 .   ? -15.944 4.005   34.369  1.00 21.31 ? 658 HOH B O   1 
HETATM 5827 O  O   . HOH F 3 .   ? 17.822  13.285  54.130  1.00 34.44 ? 659 HOH B O   1 
HETATM 5828 O  O   . HOH F 3 .   ? 12.964  18.471  29.004  1.00 31.36 ? 660 HOH B O   1 
HETATM 5829 O  O   . HOH F 3 .   ? 6.349   11.366  28.596  1.00 28.32 ? 661 HOH B O   1 
HETATM 5830 O  O   . HOH F 3 .   ? -6.000  9.666   16.623  1.00 20.65 ? 662 HOH B O   1 
HETATM 5831 O  O   . HOH F 3 .   ? -2.958  -5.580  19.116  1.00 11.89 ? 663 HOH B O   1 
HETATM 5832 O  O   . HOH F 3 .   ? 20.410  -2.196  55.077  1.00 25.61 ? 664 HOH B O   1 
HETATM 5833 O  O   . HOH F 3 .   ? 13.017  10.970  41.555  1.00 22.98 ? 665 HOH B O   1 
HETATM 5834 O  O   . HOH F 3 .   ? 9.438   5.492   22.594  1.00 26.61 ? 666 HOH B O   1 
HETATM 5835 O  O   . HOH F 3 .   ? -9.654  19.819  35.706  1.00 20.49 ? 667 HOH B O   1 
HETATM 5836 O  O   . HOH F 3 .   ? 7.067   -3.006  35.768  1.00 31.51 ? 668 HOH B O   1 
HETATM 5837 O  O   . HOH F 3 .   ? -2.020  -1.173  7.290   1.00 30.47 ? 669 HOH B O   1 
HETATM 5838 O  O   . HOH F 3 .   ? 14.541  -6.234  50.505  1.00 23.32 ? 670 HOH B O   1 
HETATM 5839 O  O   . HOH F 3 .   ? 8.314   21.555  37.103  1.00 35.14 ? 671 HOH B O   1 
HETATM 5840 O  O   . HOH F 3 .   ? 17.599  -14.201 29.684  1.00 31.07 ? 672 HOH B O   1 
HETATM 5841 O  O   . HOH F 3 .   ? -23.657 15.772  23.181  1.00 41.13 ? 673 HOH B O   1 
HETATM 5842 O  O   . HOH F 3 .   ? 15.442  10.742  42.766  1.00 18.89 ? 674 HOH B O   1 
HETATM 5843 O  O   . HOH F 3 .   ? -11.198 -10.083 25.282  1.00 28.21 ? 675 HOH B O   1 
HETATM 5844 O  O   . HOH F 3 .   ? 15.873  1.673   33.211  1.00 18.29 ? 676 HOH B O   1 
HETATM 5845 O  O   . HOH F 3 .   ? -11.945 -5.101  7.010   1.00 27.37 ? 677 HOH B O   1 
HETATM 5846 O  O   . HOH F 3 .   ? 27.013  6.276   25.205  1.00 27.53 ? 678 HOH B O   1 
HETATM 5847 O  O   . HOH F 3 .   ? 25.187  11.503  44.110  1.00 29.75 ? 679 HOH B O   1 
HETATM 5848 O  O   . HOH F 3 .   ? -12.918 18.486  41.873  1.00 36.92 ? 680 HOH B O   1 
HETATM 5849 O  O   . HOH F 3 .   ? -8.839  -7.119  36.126  1.00 30.51 ? 681 HOH B O   1 
HETATM 5850 O  O   . HOH F 3 .   ? -14.338 1.852   32.902  1.00 20.85 ? 682 HOH B O   1 
HETATM 5851 O  O   . HOH F 3 .   ? -4.514  -10.725 26.564  1.00 12.42 ? 683 HOH B O   1 
HETATM 5852 O  O   . HOH F 3 .   ? 7.778   -8.072  17.641  1.00 34.11 ? 684 HOH B O   1 
HETATM 5853 O  O   . HOH F 3 .   ? 7.053   0.477   45.459  1.00 16.35 ? 685 HOH B O   1 
HETATM 5854 O  O   . HOH F 3 .   ? 3.023   -12.628 19.444  1.00 26.83 ? 686 HOH B O   1 
HETATM 5855 O  O   . HOH F 3 .   ? 2.800   -14.073 25.772  1.00 30.27 ? 687 HOH B O   1 
HETATM 5856 O  O   . HOH F 3 .   ? -24.536 5.370   26.932  1.00 46.14 ? 688 HOH B O   1 
HETATM 5857 O  O   . HOH F 3 .   ? -14.607 -0.977  17.434  1.00 24.33 ? 689 HOH B O   1 
HETATM 5858 O  O   . HOH F 3 .   ? 16.716  19.606  46.385  1.00 27.62 ? 690 HOH B O   1 
HETATM 5859 O  O   . HOH F 3 .   ? 1.578   14.771  18.274  1.00 19.98 ? 691 HOH B O   1 
HETATM 5860 O  O   . HOH F 3 .   ? -8.060  0.762   12.719  1.00 16.83 ? 692 HOH B O   1 
HETATM 5861 O  O   . HOH F 3 .   ? 17.352  -5.230  45.050  1.00 16.19 ? 693 HOH B O   1 
HETATM 5862 O  O   . HOH F 3 .   ? 6.740   -2.780  49.907  1.00 26.75 ? 694 HOH B O   1 
HETATM 5863 O  O   . HOH F 3 .   ? -3.927  -8.145  19.389  1.00 12.44 ? 695 HOH B O   1 
HETATM 5864 O  O   . HOH F 3 .   ? 14.995  -9.785  56.572  1.00 36.16 ? 696 HOH B O   1 
HETATM 5865 O  O   . HOH F 3 .   ? -2.992  18.006  29.339  1.00 28.82 ? 697 HOH B O   1 
HETATM 5866 O  O   . HOH F 3 .   ? 18.783  -3.191  43.771  1.00 16.68 ? 698 HOH B O   1 
HETATM 5867 O  O   . HOH F 3 .   ? -2.467  17.933  21.012  1.00 29.17 ? 699 HOH B O   1 
HETATM 5868 O  O   . HOH F 3 .   ? 12.682  16.389  39.862  1.00 28.73 ? 700 HOH B O   1 
HETATM 5869 O  O   . HOH F 3 .   ? 7.974   -0.585  48.886  1.00 16.21 ? 701 HOH B O   1 
HETATM 5870 O  O   . HOH F 3 .   ? -0.337  -15.274 23.785  1.00 25.62 ? 702 HOH B O   1 
HETATM 5871 O  O   . HOH F 3 .   ? 30.518  10.103  37.641  1.00 33.56 ? 703 HOH B O   1 
HETATM 5872 O  O   . HOH F 3 .   ? 1.293   22.435  40.197  1.00 39.92 ? 704 HOH B O   1 
HETATM 5873 O  O   . HOH F 3 .   ? -15.521 0.750   48.058  1.00 30.85 ? 705 HOH B O   1 
HETATM 5874 O  O   . HOH F 3 .   ? -8.996  -4.518  31.322  1.00 12.83 ? 706 HOH B O   1 
HETATM 5875 O  O   . HOH F 3 .   ? -2.313  6.405   48.050  1.00 22.54 ? 707 HOH B O   1 
HETATM 5876 O  O   . HOH F 3 .   ? 14.715  15.867  37.820  1.00 18.55 ? 708 HOH B O   1 
HETATM 5877 O  O   . HOH F 3 .   ? 25.631  11.414  30.460  1.00 27.54 ? 709 HOH B O   1 
HETATM 5878 O  O   . HOH F 3 .   ? -8.697  -10.258 9.671   1.00 26.81 ? 710 HOH B O   1 
HETATM 5879 O  O   . HOH F 3 .   ? 0.246   5.457   50.586  1.00 21.93 ? 711 HOH B O   1 
HETATM 5880 O  O   . HOH F 3 .   ? -4.143  16.613  31.901  1.00 22.69 ? 712 HOH B O   1 
HETATM 5881 O  O   . HOH F 3 .   ? 19.087  18.447  46.335  1.00 32.76 ? 713 HOH B O   1 
HETATM 5882 O  O   . HOH F 3 .   ? 2.510   -0.696  33.530  1.00 14.83 ? 714 HOH B O   1 
HETATM 5883 O  O   . HOH F 3 .   ? -3.134  -11.162 16.579  1.00 22.13 ? 715 HOH B O   1 
HETATM 5884 O  O   . HOH F 3 .   ? 11.544  16.328  45.288  1.00 22.72 ? 716 HOH B O   1 
HETATM 5885 O  O   . HOH F 3 .   ? -9.318  18.870  27.326  1.00 31.30 ? 717 HOH B O   1 
HETATM 5886 O  O   . HOH F 3 .   ? -6.468  -7.962  28.755  1.00 12.43 ? 718 HOH B O   1 
HETATM 5887 O  O   . HOH F 3 .   ? 12.268  2.349   24.342  1.00 20.22 ? 719 HOH B O   1 
HETATM 5888 O  O   . HOH F 3 .   ? -2.592  14.092  32.207  1.00 13.58 ? 720 HOH B O   1 
HETATM 5889 O  O   . HOH F 3 .   ? -20.397 3.946   19.475  1.00 22.77 ? 721 HOH B O   1 
HETATM 5890 O  O   . HOH F 3 .   ? -22.992 19.152  37.004  1.00 36.26 ? 722 HOH B O   1 
HETATM 5891 O  O   . HOH F 3 .   ? 18.800  8.211   17.752  1.00 29.80 ? 723 HOH B O   1 
HETATM 5892 O  O   . HOH F 3 .   ? -9.377  -0.298  37.560  1.00 14.96 ? 724 HOH B O   1 
HETATM 5893 O  O   . HOH F 3 .   ? -3.687  -7.338  12.690  1.00 14.45 ? 725 HOH B O   1 
HETATM 5894 O  O   . HOH F 3 .   ? -15.864 -6.552  20.457  1.00 25.37 ? 726 HOH B O   1 
HETATM 5895 O  O   . HOH F 3 .   ? 24.617  -5.595  50.574  1.00 32.61 ? 727 HOH B O   1 
HETATM 5896 O  O   . HOH F 3 .   ? -2.840  5.482   13.765  1.00 16.21 ? 728 HOH B O   1 
HETATM 5897 O  O   . HOH F 3 .   ? -18.690 3.229   40.598  1.00 43.23 ? 729 HOH B O   1 
HETATM 5898 O  O   . HOH F 3 .   ? -13.880 -3.994  16.974  1.00 23.09 ? 730 HOH B O   1 
HETATM 5899 O  O   . HOH F 3 .   ? -17.185 21.694  30.319  1.00 27.61 ? 731 HOH B O   1 
HETATM 5900 O  O   . HOH F 3 .   ? 17.261  -7.820  33.909  1.00 22.23 ? 732 HOH B O   1 
HETATM 5901 O  O   . HOH F 3 .   ? 14.036  14.027  42.145  1.00 29.74 ? 733 HOH B O   1 
HETATM 5902 O  O   . HOH F 3 .   ? -5.269  -7.975  16.926  1.00 21.18 ? 734 HOH B O   1 
HETATM 5903 O  O   . HOH F 3 .   ? -10.503 -7.131  38.343  1.00 29.05 ? 735 HOH B O   1 
HETATM 5904 O  O   . HOH F 3 .   ? -22.701 -0.179  31.820  1.00 35.56 ? 736 HOH B O   1 
HETATM 5905 O  O   . HOH F 3 .   ? -23.357 8.779   22.531  1.00 21.88 ? 737 HOH B O   1 
HETATM 5906 O  O   . HOH F 3 .   ? -4.615  19.589  42.553  1.00 29.18 ? 738 HOH B O   1 
HETATM 5907 O  O   . HOH F 3 .   ? -17.821 -5.506  22.031  1.00 24.90 ? 739 HOH B O   1 
HETATM 5908 O  O   . HOH F 3 .   ? -9.499  -11.845 14.133  1.00 37.40 ? 740 HOH B O   1 
HETATM 5909 O  O   . HOH F 3 .   ? 25.853  2.100   51.274  1.00 27.11 ? 741 HOH B O   1 
HETATM 5910 O  O   . HOH F 3 .   ? 9.894   21.743  34.617  1.00 22.61 ? 742 HOH B O   1 
HETATM 5911 O  O   . HOH F 3 .   ? 7.848   -5.669  41.544  1.00 35.15 ? 743 HOH B O   1 
HETATM 5912 O  O   . HOH F 3 .   ? 16.591  -13.003 48.174  1.00 25.77 ? 744 HOH B O   1 
HETATM 5913 O  O   . HOH F 3 .   ? 21.005  -4.759  42.348  1.00 18.23 ? 745 HOH B O   1 
HETATM 5914 O  O   . HOH F 3 .   ? -4.086  -13.542 13.560  1.00 34.46 ? 746 HOH B O   1 
HETATM 5915 O  O   . HOH F 3 .   ? 0.361   17.610  37.290  1.00 21.11 ? 747 HOH B O   1 
HETATM 5916 O  O   . HOH F 3 .   ? -2.523  -10.260 18.896  1.00 16.31 ? 748 HOH B O   1 
HETATM 5917 O  O   . HOH F 3 .   ? 23.822  3.763   51.129  1.00 18.94 ? 749 HOH B O   1 
HETATM 5918 O  O   . HOH F 3 .   ? -6.410  0.417   7.184   1.00 40.06 ? 750 HOH B O   1 
HETATM 5919 O  O   . HOH F 3 .   ? 27.869  1.152   35.350  1.00 29.50 ? 751 HOH B O   1 
HETATM 5920 O  O   . HOH F 3 .   ? -6.908  -5.230  29.254  1.00 13.96 ? 752 HOH B O   1 
HETATM 5921 O  O   . HOH F 3 .   ? 6.431   1.812   48.068  1.00 16.20 ? 753 HOH B O   1 
HETATM 5922 O  O   . HOH F 3 .   ? 30.790  6.324   30.446  1.00 22.75 ? 754 HOH B O   1 
HETATM 5923 O  O   . HOH F 3 .   ? 17.474  15.353  39.375  1.00 27.87 ? 755 HOH B O   1 
HETATM 5924 O  O   . HOH F 3 .   ? -12.656 -11.011 29.825  1.00 30.48 ? 756 HOH B O   1 
HETATM 5925 O  O   . HOH F 3 .   ? 15.223  -0.172  59.189  1.00 30.88 ? 757 HOH B O   1 
HETATM 5926 O  O   . HOH F 3 .   ? -16.663 19.612  18.445  1.00 34.47 ? 758 HOH B O   1 
HETATM 5927 O  O   . HOH F 3 .   ? 6.703   -1.740  53.534  1.00 29.04 ? 759 HOH B O   1 
HETATM 5928 O  O   . HOH F 3 .   ? 9.029   -7.057  32.631  1.00 29.16 ? 760 HOH B O   1 
HETATM 5929 O  O   . HOH F 3 .   ? 24.186  8.193   48.946  1.00 25.99 ? 761 HOH B O   1 
HETATM 5930 O  O   . HOH F 3 .   ? 7.976   2.544   37.891  1.00 17.21 ? 762 HOH B O   1 
HETATM 5931 O  O   . HOH F 3 .   ? -10.693 -6.078  4.482   1.00 22.35 ? 763 HOH B O   1 
HETATM 5932 O  O   . HOH F 3 .   ? -18.986 10.159  41.376  1.00 28.63 ? 764 HOH B O   1 
HETATM 5933 O  O   . HOH F 3 .   ? -11.045 11.369  45.223  1.00 20.31 ? 765 HOH B O   1 
HETATM 5934 O  O   . HOH F 3 .   ? 23.481  10.065  50.750  1.00 32.27 ? 766 HOH B O   1 
HETATM 5935 O  O   . HOH F 3 .   ? 6.187   11.333  21.898  1.00 19.63 ? 767 HOH B O   1 
HETATM 5936 O  O   . HOH F 3 .   ? -7.863  5.903   8.273   1.00 25.37 ? 768 HOH B O   1 
HETATM 5937 O  O   . HOH F 3 .   ? 25.155  -0.224  49.425  1.00 24.98 ? 769 HOH B O   1 
HETATM 5938 O  O   . HOH F 3 .   ? 10.996  -2.673  33.916  1.00 33.61 ? 770 HOH B O   1 
HETATM 5939 O  O   . HOH F 3 .   ? 10.847  18.113  47.208  1.00 29.94 ? 771 HOH B O   1 
HETATM 5940 O  O   . HOH F 3 .   ? -5.701  -11.792 14.313  1.00 32.14 ? 772 HOH B O   1 
HETATM 5941 O  O   . HOH F 3 .   ? -23.287 6.002   22.458  1.00 27.76 ? 773 HOH B O   1 
HETATM 5942 O  O   . HOH F 3 .   ? -13.087 -9.285  38.774  1.00 36.74 ? 774 HOH B O   1 
HETATM 5943 O  O   . HOH F 3 .   ? 1.187   17.204  33.159  1.00 41.42 ? 775 HOH B O   1 
HETATM 5944 O  O   . HOH F 3 .   ? -1.114  15.696  33.835  1.00 26.07 ? 776 HOH B O   1 
HETATM 5945 O  O   . HOH F 3 .   ? 7.230   10.478  26.120  1.00 40.59 ? 777 HOH B O   1 
HETATM 5946 O  O   . HOH F 3 .   ? 2.317   -7.788  39.321  1.00 38.97 ? 778 HOH B O   1 
HETATM 5947 O  O   . HOH F 3 .   ? -4.631  -9.172  14.569  1.00 20.76 ? 779 HOH B O   1 
HETATM 5948 O  O   . HOH F 3 .   ? 7.604   -5.067  49.796  1.00 33.10 ? 780 HOH B O   1 
HETATM 5949 O  O   . HOH F 3 .   ? -15.423 -8.971  20.929  1.00 32.81 ? 781 HOH B O   1 
HETATM 5950 O  O   . HOH F 3 .   ? 10.110  1.337   38.332  1.00 31.85 ? 782 HOH B O   1 
HETATM 5951 O  O   . HOH F 3 .   ? -6.843  -7.085  38.196  1.00 26.51 ? 783 HOH B O   1 
HETATM 5952 O  O   . HOH F 3 .   ? -24.573 9.912   24.644  1.00 38.89 ? 784 HOH B O   1 
# 
